The CC domain structure from the wheat stem rust resistance protein Sr33 challenges paradigms for dimerization in plant NLR proteins.
Identifieur interne : 000077 ( Main/Exploration ); précédent : 000076; suivant : 000078The CC domain structure from the wheat stem rust resistance protein Sr33 challenges paradigms for dimerization in plant NLR proteins.
Auteurs : Lachlan W. Casey [Australie] ; Peter Lavrencic [Australie] ; Adam R. Bentham [Australie] ; Stella Cesari [Australie] ; Daniel J. Ericsson [Australie] ; Tristan Croll [Australie] ; Dušan Turk [Slovénie] ; Peter A. Anderson [Australie] ; Alan E. Mark [Australie] ; Peter N. Dodds [Australie] ; Mehdi Mobli [Australie] ; Bostjan Kobe [Australie] ; Simon J. Williams [Australie]Source :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2016.
Abstract
Plants use intracellular immunity receptors, known as nucleotide-binding oligomerization domain-like receptors (NLRs), to recognize specific pathogen effector proteins and induce immune responses. These proteins provide resistance to many of the world's most destructive plant pathogens, yet we have a limited understanding of the molecular mechanisms that lead to defense signaling. We examined the wheat NLR protein, Sr33, which is responsible for strain-specific resistance to the wheat stem rust pathogen, Puccinia graminis f. sp. tritici We present the solution structure of a coiled-coil (CC) fragment from Sr33, which adopts a four-helix bundle conformation. Unexpectedly, this structure differs from the published dimeric crystal structure of the equivalent region from the orthologous barley powdery mildew resistance protein, MLA10, but is similar to the structure of the distantly related potato NLR protein, Rx. We demonstrate that these regions are, in fact, largely monomeric and adopt similar folds in solution in all three proteins, suggesting that the CC domains from plant NLRs adopt a conserved fold. However, larger C-terminal fragments of Sr33 and MLA10 can self-associate both in vitro and in planta, and this self-association correlates with their cell death signaling activity. The minimal region of the CC domain required for both cell death signaling and self-association extends to amino acid 142, thus including 22 residues absent from previous biochemical and structural protein studies. These data suggest that self-association of the minimal CC domain is necessary for signaling but is likely to involve a different structural basis than previously suggested by the MLA10 crystallographic dimer.
DOI: 10.1073/pnas.1609922113
PubMed: 27791121
PubMed Central: PMC5111715
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Mark</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072</wicri:regionArea><wicri:noRegion>QLD 4072</wicri:noRegion></affiliation></author><author><name sortKey="Dodds, Peter N" sort="Dodds, Peter N" uniqKey="Dodds P" first="Peter N" last="Dodds">Peter N. Dodds</name><affiliation wicri:level="1"><nlm:affiliation>Commonwealth Scientific and Industrial Research Organization Agriculture, Canberra, ACT 2601, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Commonwealth Scientific and Industrial Research Organization Agriculture, Canberra, ACT 2601</wicri:regionArea><wicri:noRegion>ACT 2601</wicri:noRegion></affiliation></author><author><name sortKey="Mobli, Mehdi" sort="Mobli, Mehdi" uniqKey="Mobli M" first="Mehdi" last="Mobli">Mehdi Mobli</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Advanced Imaging, University of Queensland, Brisbane, QLD 4072, Australia; s.williams8@uq.edu.au m.mobli@uq.edu.au b.kobe@uq.edu.au.</nlm:affiliation><country wicri:rule="url">Australie</country><wicri:regionArea>Centre for Advanced Imaging, University of Queensland, Brisbane, QLD 4072</wicri:regionArea><wicri:noRegion>QLD 4072</wicri:noRegion></affiliation></author><author><name sortKey="Kobe, Bostjan" sort="Kobe, Bostjan" uniqKey="Kobe B" first="Bostjan" last="Kobe">Bostjan Kobe</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia; s.williams8@uq.edu.au m.mobli@uq.edu.au b.kobe@uq.edu.au.</nlm:affiliation><country wicri:rule="url">Australie</country><wicri:regionArea>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072</wicri:regionArea><wicri:noRegion>QLD 4072</wicri:noRegion></affiliation></author><author><name sortKey="Williams, Simon J" sort="Williams, Simon J" uniqKey="Williams S" first="Simon J" last="Williams">Simon J. 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Casey</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072</wicri:regionArea><wicri:noRegion>QLD 4072</wicri:noRegion></affiliation></author><author><name sortKey="Lavrencic, Peter" sort="Lavrencic, Peter" uniqKey="Lavrencic P" first="Peter" last="Lavrencic">Peter Lavrencic</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072</wicri:regionArea><wicri:noRegion>QLD 4072</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Centre for Advanced Imaging, University of Queensland, Brisbane, QLD 4072, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Centre for Advanced Imaging, University of Queensland, Brisbane, QLD 4072</wicri:regionArea><wicri:noRegion>QLD 4072</wicri:noRegion></affiliation></author><author><name sortKey="Bentham, Adam R" sort="Bentham, Adam R" uniqKey="Bentham A" first="Adam R" last="Bentham">Adam R. Bentham</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072</wicri:regionArea><wicri:noRegion>QLD 4072</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>School of Biological Sciences, Flinders University, Adelaide, SA 5001, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Biological Sciences, Flinders University, Adelaide, SA 5001</wicri:regionArea><wicri:noRegion>SA 5001</wicri:noRegion></affiliation></author><author><name sortKey="Cesari, Stella" sort="Cesari, Stella" uniqKey="Cesari S" first="Stella" last="Cesari">Stella Cesari</name><affiliation wicri:level="1"><nlm:affiliation>Commonwealth Scientific and Industrial Research Organization Agriculture, Canberra, ACT 2601, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Commonwealth Scientific and Industrial Research Organization Agriculture, Canberra, ACT 2601</wicri:regionArea><wicri:noRegion>ACT 2601</wicri:noRegion></affiliation></author><author><name sortKey="Ericsson, Daniel J" sort="Ericsson, Daniel J" uniqKey="Ericsson D" first="Daniel J" last="Ericsson">Daniel J. Ericsson</name><affiliation wicri:level="1"><nlm:affiliation>Macromolecular Crystallography (MX) Beamlines, Australian Synchrotron, Melbourne, VIC 3168, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Macromolecular Crystallography (MX) Beamlines, Australian Synchrotron, Melbourne, VIC 3168</wicri:regionArea><wicri:noRegion>VIC 3168</wicri:noRegion></affiliation></author><author><name sortKey="Croll, Tristan" sort="Croll, Tristan" uniqKey="Croll T" first="Tristan" last="Croll">Tristan Croll</name><affiliation wicri:level="1"><nlm:affiliation>School of Biomedical Sciences, Queensland University of Technology, Brisbane, QLD 4001, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Biomedical Sciences, Queensland University of Technology, Brisbane, QLD 4001</wicri:regionArea><wicri:noRegion>QLD 4001</wicri:noRegion></affiliation></author><author><name sortKey="Turk, Dusan" sort="Turk, Dusan" uniqKey="Turk D" first="Dušan" last="Turk">Dušan Turk</name><affiliation wicri:level="1"><nlm:affiliation>Centre of Excellence for Integrated Approaches in Chemistry and Biology of Proteins, International Postgraduate School Jozef Stefan, Jozef Stefan Institute, 1000 Ljubljana, Slovenia.</nlm:affiliation><country xml:lang="fr">Slovénie</country><wicri:regionArea>Centre of Excellence for Integrated Approaches in Chemistry and Biology of Proteins, International Postgraduate School Jozef Stefan, Jozef Stefan Institute, 1000 Ljubljana</wicri:regionArea><wicri:noRegion>1000 Ljubljana</wicri:noRegion></affiliation></author><author><name sortKey="Anderson, Peter A" sort="Anderson, Peter A" uniqKey="Anderson P" first="Peter A" last="Anderson">Peter A. Anderson</name><affiliation wicri:level="1"><nlm:affiliation>School of Biological Sciences, Flinders University, Adelaide, SA 5001, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Biological Sciences, Flinders University, Adelaide, SA 5001</wicri:regionArea><wicri:noRegion>SA 5001</wicri:noRegion></affiliation></author><author><name sortKey="Mark, Alan E" sort="Mark, Alan E" uniqKey="Mark A" first="Alan E" last="Mark">Alan E. Mark</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072</wicri:regionArea><wicri:noRegion>QLD 4072</wicri:noRegion></affiliation></author><author><name sortKey="Dodds, Peter N" sort="Dodds, Peter N" uniqKey="Dodds P" first="Peter N" last="Dodds">Peter N. Dodds</name><affiliation wicri:level="1"><nlm:affiliation>Commonwealth Scientific and Industrial Research Organization Agriculture, Canberra, ACT 2601, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Commonwealth Scientific and Industrial Research Organization Agriculture, Canberra, ACT 2601</wicri:regionArea><wicri:noRegion>ACT 2601</wicri:noRegion></affiliation></author><author><name sortKey="Mobli, Mehdi" sort="Mobli, Mehdi" uniqKey="Mobli M" first="Mehdi" last="Mobli">Mehdi Mobli</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Advanced Imaging, University of Queensland, Brisbane, QLD 4072, Australia; s.williams8@uq.edu.au m.mobli@uq.edu.au b.kobe@uq.edu.au.</nlm:affiliation><country wicri:rule="url">Australie</country><wicri:regionArea>Centre for Advanced Imaging, University of Queensland, Brisbane, QLD 4072</wicri:regionArea><wicri:noRegion>QLD 4072</wicri:noRegion></affiliation></author><author><name sortKey="Kobe, Bostjan" sort="Kobe, Bostjan" uniqKey="Kobe B" first="Bostjan" last="Kobe">Bostjan Kobe</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia; s.williams8@uq.edu.au m.mobli@uq.edu.au b.kobe@uq.edu.au.</nlm:affiliation><country wicri:rule="url">Australie</country><wicri:regionArea>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072</wicri:regionArea><wicri:noRegion>QLD 4072</wicri:noRegion></affiliation></author><author><name sortKey="Williams, Simon J" sort="Williams, Simon J" uniqKey="Williams S" first="Simon J" last="Williams">Simon J. Williams</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia; s.williams8@uq.edu.au m.mobli@uq.edu.au b.kobe@uq.edu.au.</nlm:affiliation><country wicri:rule="url">Australie</country><wicri:regionArea>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072</wicri:regionArea><wicri:noRegion>QLD 4072</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>School of Biological Sciences, Flinders University, Adelaide, SA 5001, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Biological Sciences, Flinders University, Adelaide, SA 5001</wicri:regionArea><wicri:noRegion>SA 5001</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Plant Sciences Division, Research School of Biology, The Australian National University, Canberra, ACT 2601, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Plant Sciences Division, Research School of Biology, The Australian National University, Canberra, ACT 2601</wicri:regionArea><wicri:noRegion>ACT 2601</wicri:noRegion></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="eISSN">1091-6490</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Plants use intracellular immunity receptors, known as nucleotide-binding oligomerization domain-like receptors (NLRs), to recognize specific pathogen effector proteins and induce immune responses. These proteins provide resistance to many of the world's most destructive plant pathogens, yet we have a limited understanding of the molecular mechanisms that lead to defense signaling. We examined the wheat NLR protein, Sr33, which is responsible for strain-specific resistance to the wheat stem rust pathogen, <i>Puccinia graminis f. sp. tritici</i> We present the solution structure of a coiled-coil (CC) fragment from Sr33, which adopts a four-helix bundle conformation. Unexpectedly, this structure differs from the published dimeric crystal structure of the equivalent region from the orthologous barley powdery mildew resistance protein, MLA10, but is similar to the structure of the distantly related potato NLR protein, Rx. We demonstrate that these regions are, in fact, largely monomeric and adopt similar folds in solution in all three proteins, suggesting that the CC domains from plant NLRs adopt a conserved fold. However, larger C-terminal fragments of Sr33 and MLA10 can self-associate both in vitro and <i>in planta</i>, and this self-association correlates with their cell death signaling activity. The minimal region of the CC domain required for both cell death signaling and self-association extends to amino acid 142, thus including 22 residues absent from previous biochemical and structural protein studies. These data suggest that self-association of the minimal CC domain is necessary for signaling but is likely to involve a different structural basis than previously suggested by the MLA10 crystallographic dimer.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">27791121</PMID><DateRevised><Year>2019</Year><Month>11</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>113</Volume><Issue>45</Issue><PubDate><Year>2016</Year><Month>Nov</Month><Day>08</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>The CC domain structure from the wheat stem rust resistance protein Sr33 challenges paradigms for dimerization in plant NLR proteins.</ArticleTitle><Pagination><MedlinePgn>12856-12861</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1609922113</ELocationID><Abstract><AbstractText>Plants use intracellular immunity receptors, known as nucleotide-binding oligomerization domain-like receptors (NLRs), to recognize specific pathogen effector proteins and induce immune responses. These proteins provide resistance to many of the world's most destructive plant pathogens, yet we have a limited understanding of the molecular mechanisms that lead to defense signaling. We examined the wheat NLR protein, Sr33, which is responsible for strain-specific resistance to the wheat stem rust pathogen, <i>Puccinia graminis f. sp. tritici</i> We present the solution structure of a coiled-coil (CC) fragment from Sr33, which adopts a four-helix bundle conformation. Unexpectedly, this structure differs from the published dimeric crystal structure of the equivalent region from the orthologous barley powdery mildew resistance protein, MLA10, but is similar to the structure of the distantly related potato NLR protein, Rx. We demonstrate that these regions are, in fact, largely monomeric and adopt similar folds in solution in all three proteins, suggesting that the CC domains from plant NLRs adopt a conserved fold. However, larger C-terminal fragments of Sr33 and MLA10 can self-associate both in vitro and <i>in planta</i>, and this self-association correlates with their cell death signaling activity. The minimal region of the CC domain required for both cell death signaling and self-association extends to amino acid 142, thus including 22 residues absent from previous biochemical and structural protein studies. These data suggest that self-association of the minimal CC domain is necessary for signaling but is likely to involve a different structural basis than previously suggested by the MLA10 crystallographic dimer.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Casey</LastName><ForeName>Lachlan W</ForeName><Initials>LW</Initials><AffiliationInfo><Affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lavrencic</LastName><ForeName>Peter</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Centre for Advanced Imaging, University of Queensland, Brisbane, QLD 4072, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bentham</LastName><ForeName>Adam R</ForeName><Initials>AR</Initials><AffiliationInfo><Affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>School of Biological Sciences, Flinders University, Adelaide, SA 5001, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cesari</LastName><ForeName>Stella</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Commonwealth Scientific and Industrial Research Organization Agriculture, Canberra, ACT 2601, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ericsson</LastName><ForeName>Daniel J</ForeName><Initials>DJ</Initials><AffiliationInfo><Affiliation>Macromolecular Crystallography (MX) Beamlines, Australian Synchrotron, Melbourne, VIC 3168, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Croll</LastName><ForeName>Tristan</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>School of Biomedical Sciences, Queensland University of Technology, Brisbane, QLD 4001, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Turk</LastName><ForeName>Dušan</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Centre of Excellence for Integrated Approaches in Chemistry and Biology of Proteins, International Postgraduate School Jozef Stefan, Jozef Stefan Institute, 1000 Ljubljana, Slovenia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Anderson</LastName><ForeName>Peter A</ForeName><Initials>PA</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Flinders University, Adelaide, SA 5001, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mark</LastName><ForeName>Alan E</ForeName><Initials>AE</Initials><AffiliationInfo><Affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dodds</LastName><ForeName>Peter N</ForeName><Initials>PN</Initials><AffiliationInfo><Affiliation>Commonwealth Scientific and Industrial Research Organization Agriculture, Canberra, ACT 2601, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mobli</LastName><ForeName>Mehdi</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Centre for Advanced Imaging, University of Queensland, Brisbane, QLD 4072, Australia; s.williams8@uq.edu.au m.mobli@uq.edu.au b.kobe@uq.edu.au.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kobe</LastName><ForeName>Bostjan</ForeName><Initials>B</Initials><Identifier Source="ORCID">http://orcid.org/0000-0001-9413-9166</Identifier><AffiliationInfo><Affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia; s.williams8@uq.edu.au m.mobli@uq.edu.au b.kobe@uq.edu.au.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Williams</LastName><ForeName>Simon J</ForeName><Initials>SJ</Initials><AffiliationInfo><Affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australia; s.williams8@uq.edu.au m.mobli@uq.edu.au b.kobe@uq.edu.au.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>School of Biological Sciences, Flinders University, Adelaide, SA 5001, Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Plant Sciences Division, Research School of Biology, The Australian National University, Canberra, ACT 2601, Australia.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>2NCG</AccessionNumber><AccessionNumber>5T1Y</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>10</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">NLR proteins</Keyword><Keyword MajorTopicYN="N">effector-triggered immunity</Keyword><Keyword MajorTopicYN="N">nuclear magnetic resonance spectroscopy</Keyword><Keyword MajorTopicYN="N">plant innate immunity</Keyword><Keyword MajorTopicYN="N">resistance protein</Keyword></KeywordList><CoiStatement>The authors declare no conflict of interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>10</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>10</Month><Day>30</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate 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