Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: biological implications for cell wall metabolism.
Identifieur interne : 003A73 ( Main/Exploration ); précédent : 003A72; suivant : 003A74Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: biological implications for cell wall metabolism.
Auteurs : Martin J. Baumann [Suède] ; Jens M. Eklöf ; Gurvan Michel ; Asa M. Kallas ; Tuula T. Teeri ; Mirjam Czjzek ; Harry BrumerSource :
- The Plant cell [ 1040-4651 ] ; 2007.
Descripteurs français
- KwdFr :
- ADN complémentaire (métabolisme), Catalyse (MeSH), Chromatographie sur gel (MeSH), Cinétique (MeSH), Clonage moléculaire (MeSH), Cristallographie aux rayons X (MeSH), Données de séquences moléculaires (MeSH), Délétion de gène (MeSH), Glucanes (MeSH), Glycosidases (composition chimique), Mutagenèse (MeSH), Oligosaccharides (métabolisme), Paroi cellulaire (métabolisme), Phylogenèse (MeSH), Protéines mutantes (composition chimique), Protéines mutantes (métabolisme), Protéines recombinantes (métabolisme), Protéines végétales (composition chimique), Relation structure-activité (MeSH), Spécificité du substrat (MeSH), Structure secondaire des protéines (MeSH), Tropaeolum (enzymologie), Xylanes (MeSH), Électricité statique (MeSH), Évolution moléculaire (MeSH).
- MESH :
- composition chimique : Glycosidases, Protéines mutantes, Protéines végétales.
- enzymologie : Tropaeolum.
- métabolisme : ADN complémentaire, Oligosaccharides, Paroi cellulaire, Protéines mutantes, Protéines recombinantes.
- Catalyse, Chromatographie sur gel, Cinétique, Clonage moléculaire, Cristallographie aux rayons X, Données de séquences moléculaires, Délétion de gène, Glucanes, Mutagenèse, Phylogenèse, Relation structure-activité, Spécificité du substrat, Structure secondaire des protéines, Xylanes, Électricité statique, Évolution moléculaire.
English descriptors
- KwdEn :
- Catalysis (MeSH), Cell Wall (metabolism), Chromatography, Gel (MeSH), Cloning, Molecular (MeSH), Crystallography, X-Ray (MeSH), DNA, Complementary (metabolism), Evolution, Molecular (MeSH), Gene Deletion (MeSH), Glucans (MeSH), Glycoside Hydrolases (chemistry), Kinetics (MeSH), Molecular Sequence Data (MeSH), Mutagenesis (MeSH), Mutant Proteins (chemistry), Mutant Proteins (metabolism), Oligosaccharides (metabolism), Phylogeny (MeSH), Plant Proteins (chemistry), Protein Structure, Secondary (MeSH), Recombinant Proteins (metabolism), Static Electricity (MeSH), Structure-Activity Relationship (MeSH), Substrate Specificity (MeSH), Tropaeolum (enzymology), Xylans (MeSH).
- MESH :
- chemical , chemistry : Glycoside Hydrolases, Mutant Proteins, Plant Proteins.
- chemical , metabolism : DNA, Complementary, Mutant Proteins, Oligosaccharides, Recombinant Proteins.
- enzymology : Tropaeolum.
- metabolism : Cell Wall.
- Catalysis, Chromatography, Gel, Cloning, Molecular, Crystallography, X-Ray, Evolution, Molecular, Gene Deletion, Glucans, Kinetics, Molecular Sequence Data, Mutagenesis, Phylogeny, Protein Structure, Secondary, Static Electricity, Structure-Activity Relationship, Substrate Specificity, Xylans.
Abstract
High-resolution, three-dimensional structures of the archetypal glycoside hydrolase family 16 (GH16) endo-xyloglucanases Tm-NXG1 and Tm-NXG2 from nasturtium (Tropaeolum majus) have been solved by x-ray crystallography. Key structural features that modulate the relative rates of substrate hydrolysis to transglycosylation in the GH16 xyloglucan-active enzymes were identified by structure-function studies of the recombinantly expressed enzymes in comparison with data for the strict xyloglucan endo-transglycosylase Ptt-XET16-34 from hybrid aspen (Populus tremula x Populus tremuloides). Production of the loop deletion variant Tm-NXG1-DeltaYNIIG yielded an enzyme that was structurally similar to Ptt-XET16-34 and had a greatly increased transglycosylation:hydrolysis ratio. Comprehensive bioinformatic analyses of XTH gene products, together with detailed kinetic data, strongly suggest that xyloglucanase activity has evolved as a gain of function in an ancestral GH16 XET to meet specific biological requirements during seed germination, fruit ripening, and rapid wall expansion.
DOI: 10.1105/tpc.107.051391
PubMed: 17557806
PubMed Central: PMC1955714
Affiliations:
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Data</term><term>Mutagenesis</term><term>Phylogeny</term><term>Protein Structure, Secondary</term><term>Static Electricity</term><term>Structure-Activity Relationship</term><term>Substrate Specificity</term><term>Xylans</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Chromatographie sur gel</term><term>Cinétique</term><term>Clonage moléculaire</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Délétion de gène</term><term>Glucanes</term><term>Mutagenèse</term><term>Phylogenèse</term><term>Relation structure-activité</term><term>Spécificité du substrat</term><term>Structure secondaire des protéines</term><term>Xylanes</term><term>Électricité statique</term><term>Évolution moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">High-resolution, three-dimensional structures of the archetypal glycoside hydrolase family 16 (GH16) endo-xyloglucanases Tm-NXG1 and Tm-NXG2 from nasturtium (Tropaeolum majus) have been solved by x-ray crystallography. Key structural features that modulate the relative rates of substrate hydrolysis to transglycosylation in the GH16 xyloglucan-active enzymes were identified by structure-function studies of the recombinantly expressed enzymes in comparison with data for the strict xyloglucan endo-transglycosylase Ptt-XET16-34 from hybrid aspen (Populus tremula x Populus tremuloides). Production of the loop deletion variant Tm-NXG1-DeltaYNIIG yielded an enzyme that was structurally similar to Ptt-XET16-34 and had a greatly increased transglycosylation:hydrolysis ratio. Comprehensive bioinformatic analyses of XTH gene products, together with detailed kinetic data, strongly suggest that xyloglucanase activity has evolved as a gain of function in an ancestral GH16 XET to meet specific biological requirements during seed germination, fruit ripening, and rapid wall expansion.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17557806</PMID><DateCompleted><Year>2007</Year><Month>10</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1040-4651</ISSN><JournalIssue CitedMedium="Print"><Volume>19</Volume><Issue>6</Issue><PubDate><Year>2007</Year><Month>Jun</Month></PubDate></JournalIssue><Title>The Plant cell</Title><ISOAbbreviation>Plant Cell</ISOAbbreviation></Journal><ArticleTitle>Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: biological implications for cell wall metabolism.</ArticleTitle><Pagination><MedlinePgn>1947-63</MedlinePgn></Pagination><Abstract><AbstractText>High-resolution, three-dimensional structures of the archetypal glycoside hydrolase family 16 (GH16) endo-xyloglucanases Tm-NXG1 and Tm-NXG2 from nasturtium (Tropaeolum majus) have been solved by x-ray crystallography. Key structural features that modulate the relative rates of substrate hydrolysis to transglycosylation in the GH16 xyloglucan-active enzymes were identified by structure-function studies of the recombinantly expressed enzymes in comparison with data for the strict xyloglucan endo-transglycosylase Ptt-XET16-34 from hybrid aspen (Populus tremula x Populus tremuloides). Production of the loop deletion variant Tm-NXG1-DeltaYNIIG yielded an enzyme that was structurally similar to Ptt-XET16-34 and had a greatly increased transglycosylation:hydrolysis ratio. Comprehensive bioinformatic analyses of XTH gene products, together with detailed kinetic data, strongly suggest that xyloglucanase activity has evolved as a gain of function in an ancestral GH16 XET to meet specific biological requirements during seed germination, fruit ripening, and rapid wall expansion.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Baumann</LastName><ForeName>Martin J</ForeName><Initials>MJ</Initials><AffiliationInfo><Affiliation>School of Biotechnology, Royal Institute of Technology, AlbaNova University Center, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Eklöf</LastName><ForeName>Jens M</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Michel</LastName><ForeName>Gurvan</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Kallas</LastName><ForeName>Asa M</ForeName><Initials>AM</Initials></Author><Author ValidYN="Y"><LastName>Teeri</LastName><ForeName>Tuula T</ForeName><Initials>TT</Initials></Author><Author ValidYN="Y"><LastName>Czjzek</LastName><ForeName>Mirjam</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Brumer</LastName><ForeName>Harry</ForeName><Initials>H</Initials><Suffix>3rd</Suffix></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AY032600</AccessionNumber><AccessionNumber>AY578086</AccessionNumber><AccessionNumber>L43094</AccessionNumber><AccessionNumber>X68254</AccessionNumber><AccessionNumber>X68255</AccessionNumber></AccessionNumberList></DataBank><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>2UWA</AccessionNumber><AccessionNumber>2UWB</AccessionNumber><AccessionNumber>2UWC</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>06</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Cell</MedlineTA><NlmUniqueID>9208688</NlmUniqueID><ISSNLinking>1040-4651</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005936">Glucans</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050505">Mutant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009844">Oligosaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014990">Xylans</NameOfSubstance></Chemical><Chemical><RegistryNumber>37294-28-3</RegistryNumber><NameOfSubstance UI="C029353">xyloglucan</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="D006026">Glycoside Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="C072818">xyloglucan endo(1-4)-beta-D-glucanase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002473" MajorTopicYN="N">Cell Wall</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002850" MajorTopicYN="N">Chromatography, Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019143" MajorTopicYN="Y">Evolution, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017353" MajorTopicYN="N">Gene Deletion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005936" MajorTopicYN="N">Glucans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006026" MajorTopicYN="N">Glycoside Hydrolases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016296" MajorTopicYN="N">Mutagenesis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050505" MajorTopicYN="N">Mutant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009844" MajorTopicYN="N">Oligosaccharides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055672" MajorTopicYN="N">Static Electricity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032388" MajorTopicYN="N">Tropaeolum</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014990" 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uniqKey="Brumer H" first="Harry" last="Brumer">Harry Brumer</name><name sortKey="Czjzek, Mirjam" sort="Czjzek, Mirjam" uniqKey="Czjzek M" first="Mirjam" last="Czjzek">Mirjam Czjzek</name><name sortKey="Eklof, Jens M" sort="Eklof, Jens M" uniqKey="Eklof J" first="Jens M" last="Eklöf">Jens M. Eklöf</name><name sortKey="Kallas, Asa M" sort="Kallas, Asa M" uniqKey="Kallas A" first="Asa M" last="Kallas">Asa M. Kallas</name><name sortKey="Michel, Gurvan" sort="Michel, Gurvan" uniqKey="Michel G" first="Gurvan" last="Michel">Gurvan Michel</name><name sortKey="Teeri, Tuula T" sort="Teeri, Tuula T" uniqKey="Teeri T" first="Tuula T" last="Teeri">Tuula T. Teeri</name></noCountry><country name="Suède"><region name="Svealand"><name sortKey="Baumann, Martin J" sort="Baumann, Martin J" uniqKey="Baumann M" first="Martin J" last="Baumann">Martin J. Baumann</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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