Structure of beta-cinnamomin, a protein toxic to some plant species.
Identifieur interne : 002556 ( Main/Exploration ); précédent : 002555; suivant : 002557Structure of beta-cinnamomin, a protein toxic to some plant species.
Auteurs : Maria L. Rodrigues [Portugal] ; Margarida Archer ; Paulo Martel ; Alain Jacquet ; Alfredo Cravador ; Maria A. CarrondoSource :
- Acta crystallographica. Section D, Biological crystallography [ 0907-4449 ] ; 2002.
Descripteurs français
- KwdFr :
- Conformation des protéines (MeSH), Cristallographie aux rayons X (MeSH), Données de séquences moléculaires (MeSH), Modèles moléculaires (MeSH), Phytophthora (composition chimique), Phytophthora (génétique), Phytophthora (pathogénicité), Plantes (effets des médicaments et des substances chimiques), Protéines (composition chimique), Protéines (génétique), Protéines (toxicité), Protéines d'algue (composition chimique), Protéines d'algue (génétique), Protéines d'algue (toxicité), Protéines fongiques (MeSH), Protéines inactivant les ribosomes de type 2 (MeSH), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Similitude de séquences d'acides aminés (MeSH), Structure moléculaire (MeSH), Séquence d'acides aminés (MeSH), Électricité statique (MeSH).
- MESH :
- composition chimique : Phytophthora, Protéines, Protéines d'algue, Protéines recombinantes.
- effets des médicaments et des substances chimiques : Plantes.
- génétique : Phytophthora, Protéines, Protéines d'algue, Protéines recombinantes.
- pathogénicité : Phytophthora.
- toxicité : Protéines, Protéines d'algue.
- Conformation des protéines, Cristallographie aux rayons X, Données de séquences moléculaires, Modèles moléculaires, Protéines fongiques, Protéines inactivant les ribosomes de type 2, Similitude de séquences d'acides aminés, Structure moléculaire, Séquence d'acides aminés, Électricité statique.
English descriptors
- KwdEn :
- Algal Proteins (chemistry), Algal Proteins (genetics), Algal Proteins (toxicity), Amino Acid Sequence (MeSH), Crystallography, X-Ray (MeSH), Fungal Proteins (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Molecular Structure (MeSH), Phytophthora (chemistry), Phytophthora (genetics), Phytophthora (pathogenicity), Plants (drug effects), Protein Conformation (MeSH), Proteins (chemistry), Proteins (genetics), Proteins (toxicity), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Ribosome Inactivating Proteins, Type 2 (MeSH), Sequence Homology, Amino Acid (MeSH), Static Electricity (MeSH).
- MESH :
- chemical , chemistry : Algal Proteins, Proteins, Recombinant Proteins.
- chemical , genetics : Algal Proteins, Proteins, Recombinant Proteins.
- chemical , toxicity : Algal Proteins, Proteins.
- chemistry : Phytophthora.
- drug effects : Plants.
- genetics : Phytophthora.
- pathogenicity : Phytophthora.
- Amino Acid Sequence, Crystallography, X-Ray, Fungal Proteins, Models, Molecular, Molecular Sequence Data, Molecular Structure, Protein Conformation, Ribosome Inactivating Proteins, Type 2, Sequence Homology, Amino Acid, Static Electricity.
Abstract
Phytophthora and Pythium species are among the most aggressive plant pathogens, as they invade many economically important crops and forest trees. They secrete large amounts of 10 kDa proteins called elicitins that can act as elicitors of plant defence mechanisms. These proteins may also induce a hypersensitive response (HR) including plant cell necrosis, with different levels of toxicity depending on their pI. Recent studies showed that elicitins function as sterol carrier proteins. The crystallographic structure of the highly necrotic recombinant beta-cinnamomin (beta-CIN) from Phytophthora cinnamomi has been determined at 1.8 A resolution using the molecular-replacement method. beta-CIN has the same overall structure as beta-cryptogein (beta-CRY), an elicitin secreted by Phytophthora cryptogea, although it shows a different surface electrostatic potential distribution. The protein was expressed in Pichia pastoris and crystallized in the triclinic space group with two monomers in the asymmetric unit. The interface formed by these two monomers resembles that from beta-CRY dimer, although with fewer interactions.
DOI: 10.1107/s0907444902010107
PubMed: 12136143
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Carrondo</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:12136143</idno><idno type="pmid">12136143</idno><idno type="doi">10.1107/s0907444902010107</idno><idno type="wicri:Area/Main/Corpus">002654</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002654</idno><idno type="wicri:Area/Main/Curation">002654</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002654</idno><idno type="wicri:Area/Main/Exploration">002654</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Structure of beta-cinnamomin, a protein toxic to some plant species.</title><author><name sortKey="Rodrigues, Maria L" sort="Rodrigues, Maria L" uniqKey="Rodrigues M" first="Maria L" last="Rodrigues">Maria L. Rodrigues</name><affiliation wicri:level="1"><nlm:affiliation>Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, ITQB-UNL, Av. República, Apt 127, 2781-901 Oeiras, Portugal.</nlm:affiliation><country xml:lang="fr">Portugal</country><wicri:regionArea>Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, ITQB-UNL, Av. 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They secrete large amounts of 10 kDa proteins called elicitins that can act as elicitors of plant defence mechanisms. These proteins may also induce a hypersensitive response (HR) including plant cell necrosis, with different levels of toxicity depending on their pI. Recent studies showed that elicitins function as sterol carrier proteins. The crystallographic structure of the highly necrotic recombinant beta-cinnamomin (beta-CIN) from Phytophthora cinnamomi has been determined at 1.8 A resolution using the molecular-replacement method. beta-CIN has the same overall structure as beta-cryptogein (beta-CRY), an elicitin secreted by Phytophthora cryptogea, although it shows a different surface electrostatic potential distribution. The protein was expressed in Pichia pastoris and crystallized in the triclinic space group with two monomers in the asymmetric unit. The interface formed by these two monomers resembles that from beta-CRY dimer, although with fewer interactions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12136143</PMID><DateCompleted><Year>2003</Year><Month>02</Month><Day>05</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>05</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0907-4449</ISSN><JournalIssue CitedMedium="Print"><Volume>58</Volume><Issue>Pt 8</Issue><PubDate><Year>2002</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Biological crystallography</Title><ISOAbbreviation>Acta Crystallogr D Biol Crystallogr</ISOAbbreviation></Journal><ArticleTitle>Structure of beta-cinnamomin, a protein toxic to some plant species.</ArticleTitle><Pagination><MedlinePgn>1314-21</MedlinePgn></Pagination><Abstract><AbstractText>Phytophthora and Pythium species are among the most aggressive plant pathogens, as they invade many economically important crops and forest trees. They secrete large amounts of 10 kDa proteins called elicitins that can act as elicitors of plant defence mechanisms. These proteins may also induce a hypersensitive response (HR) including plant cell necrosis, with different levels of toxicity depending on their pI. Recent studies showed that elicitins function as sterol carrier proteins. The crystallographic structure of the highly necrotic recombinant beta-cinnamomin (beta-CIN) from Phytophthora cinnamomi has been determined at 1.8 A resolution using the molecular-replacement method. beta-CIN has the same overall structure as beta-cryptogein (beta-CRY), an elicitin secreted by Phytophthora cryptogea, although it shows a different surface electrostatic potential distribution. The protein was expressed in Pichia pastoris and crystallized in the triclinic space group with two monomers in the asymmetric unit. The interface formed by these two monomers resembles that from beta-CRY dimer, although with fewer interactions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rodrigues</LastName><ForeName>Maria L</ForeName><Initials>ML</Initials><AffiliationInfo><Affiliation>Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, ITQB-UNL, Av. República, Apt 127, 2781-901 Oeiras, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Archer</LastName><ForeName>Margarida</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Martel</LastName><ForeName>Paulo</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Jacquet</LastName><ForeName>Alain</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Cravador</LastName><ForeName>Alfredo</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Carrondo</LastName><ForeName>Maria A</ForeName><Initials>MA</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2002</Year><Month>07</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Acta Crystallogr D Biol Crystallogr</MedlineTA><NlmUniqueID>9305878</NlmUniqueID><ISSNLinking>0907-4449</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020418">Algal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054790">Ribosome Inactivating Proteins, Type 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C061032">cryptogein protein, Phytophthora cryptogea</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C085101">elicitin, Phytophthora</NameOfSubstance></Chemical><Chemical><RegistryNumber>115742-69-3</RegistryNumber><NameOfSubstance UI="C061930">cinnamomin, Phytophthora cinnamomi</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020418" MajorTopicYN="N">Algal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010838" MajorTopicYN="N">Phytophthora</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000472" MajorTopicYN="N">pathogenicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054790" MajorTopicYN="N">Ribosome Inactivating Proteins, Type 2</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055672" MajorTopicYN="N">Static Electricity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2002</Year><Month>02</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2002</Year><Month>06</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>7</Month><Day>24</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>2</Month><Day>6</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>7</Month><Day>24</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12136143</ArticleId><ArticleId IdType="pii">S0907444902010107</ArticleId><ArticleId IdType="doi">10.1107/s0907444902010107</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Portugal</li></country></list><tree><noCountry><name sortKey="Archer, Margarida" sort="Archer, Margarida" uniqKey="Archer M" first="Margarida" last="Archer">Margarida Archer</name><name sortKey="Carrondo, Maria A" sort="Carrondo, Maria A" uniqKey="Carrondo M" first="Maria A" last="Carrondo">Maria A. Carrondo</name><name sortKey="Cravador, Alfredo" sort="Cravador, Alfredo" uniqKey="Cravador A" first="Alfredo" last="Cravador">Alfredo Cravador</name><name sortKey="Jacquet, Alain" sort="Jacquet, Alain" uniqKey="Jacquet A" first="Alain" last="Jacquet">Alain Jacquet</name><name sortKey="Martel, Paulo" sort="Martel, Paulo" uniqKey="Martel P" first="Paulo" last="Martel">Paulo Martel</name></noCountry><country name="Portugal"><noRegion><name sortKey="Rodrigues, Maria L" sort="Rodrigues, Maria L" uniqKey="Rodrigues M" first="Maria L" last="Rodrigues">Maria L. Rodrigues</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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