Structure of sylvaticin, a new alpha-elicitin-like protein from Pythium sylvaticum.
Identifieur interne : 001D85 ( Main/Exploration ); précédent : 001D84; suivant : 001D86Structure of sylvaticin, a new alpha-elicitin-like protein from Pythium sylvaticum.
Auteurs : Marie-Bernard Lascombe [France] ; Pascal Retailleau ; Michel Ponchet ; Benoît Industri ; Jean-Pierre Blein ; Thierry PrangéSource :
- Acta crystallographica. Section D, Biological crystallography [ 0907-4449 ] ; 2007.
Descripteurs français
- KwdFr :
- Conformation des protéines (MeSH), Conformation moléculaire (MeSH), Cristallisation (MeSH), Cristallographie aux rayons X (méthodes), Données de séquences moléculaires (MeSH), Furanes (composition chimique), Modèles moléculaires (MeSH), Protéines (MeSH), Protéines d'algue (composition chimique), Pythium (métabolisme), Solvants (composition chimique), Structure secondaire des protéines (MeSH), Stérols (composition chimique), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Furanes, Protéines d'algue, Solvants, Stérols.
- métabolisme : Pythium.
- méthodes : Cristallographie aux rayons X.
- Conformation des protéines, Conformation moléculaire, Cristallisation, Données de séquences moléculaires, Modèles moléculaires, Protéines, Structure secondaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Algal Proteins (chemistry), Amino Acid Sequence (MeSH), Crystallization (MeSH), Crystallography, X-Ray (methods), Furans (chemistry), Models, Molecular (MeSH), Molecular Conformation (MeSH), Molecular Sequence Data (MeSH), Protein Conformation (MeSH), Protein Structure, Secondary (MeSH), Proteins (MeSH), Pythium (metabolism), Solvents (chemistry), Sterols (chemistry).
- MESH :
- chemical , chemistry : Algal Proteins, Furans, Solvents, Sterols.
- metabolism : Pythium.
- methods : Crystallography, X-Ray.
- Amino Acid Sequence, Crystallization, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Proteins.
Abstract
The structure of sylvaticin, a 10 kDa major pythin protein excreted by the parasitic oomycete Pythium sylvaticum, has been determined. Although closely related to alpha-elicitins in its biological response, toxicity and overall structure, sylvaticin presents a number of structural features that make it an unusual member of the elicitin class. Elicitins possess a large hydrophobic cavity and the mechanism of the systemic acquired resistance induced in planta is known to proceed through lipid transport and complexation within this cavity. Unlike other elicitins, sylvaticin contains tryptophan residues, one of which points inwards towards the central cavity, thus limiting access to sterols. In the case of sylvaticin, the sterol-transport mechanism is likely to be of less importance compared with other members of the elicitin family and still remains to be fully characterized.
DOI: 10.1107/S0907444907043363
PubMed: 17881828
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Section D, Biological crystallography</title><idno type="ISSN">0907-4449</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Algal Proteins (chemistry)</term><term>Amino Acid Sequence (MeSH)</term><term>Crystallization (MeSH)</term><term>Crystallography, X-Ray (methods)</term><term>Furans (chemistry)</term><term>Models, Molecular (MeSH)</term><term>Molecular Conformation (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Protein Structure, Secondary (MeSH)</term><term>Proteins (MeSH)</term><term>Pythium (metabolism)</term><term>Solvents (chemistry)</term><term>Sterols (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines (MeSH)</term><term>Conformation moléculaire (MeSH)</term><term>Cristallisation (MeSH)</term><term>Cristallographie aux rayons X (méthodes)</term><term>Données de séquences moléculaires (MeSH)</term><term>Furanes (composition chimique)</term><term>Modèles moléculaires (MeSH)</term><term>Protéines (MeSH)</term><term>Protéines d'algue (composition chimique)</term><term>Pythium (métabolisme)</term><term>Solvants (composition chimique)</term><term>Structure secondaire des protéines (MeSH)</term><term>Stérols (composition chimique)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Algal Proteins</term><term>Furans</term><term>Solvents</term><term>Sterols</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Furanes</term><term>Protéines d'algue</term><term>Solvants</term><term>Stérols</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Pythium</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Crystallography, X-Ray</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Pythium</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Cristallographie aux rayons X</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Crystallization</term><term>Models, Molecular</term><term>Molecular Conformation</term><term>Molecular Sequence Data</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Proteins</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Conformation moléculaire</term><term>Cristallisation</term><term>Données de séquences moléculaires</term><term>Modèles moléculaires</term><term>Protéines</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The structure of sylvaticin, a 10 kDa major pythin protein excreted by the parasitic oomycete Pythium sylvaticum, has been determined. Although closely related to alpha-elicitins in its biological response, toxicity and overall structure, sylvaticin presents a number of structural features that make it an unusual member of the elicitin class. Elicitins possess a large hydrophobic cavity and the mechanism of the systemic acquired resistance induced in planta is known to proceed through lipid transport and complexation within this cavity. Unlike other elicitins, sylvaticin contains tryptophan residues, one of which points inwards towards the central cavity, thus limiting access to sterols. In the case of sylvaticin, the sterol-transport mechanism is likely to be of less importance compared with other members of the elicitin family and still remains to be fully characterized.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17881828</PMID><DateCompleted><Year>2007</Year><Month>12</Month><Day>12</Day></DateCompleted><DateRevised><Year>2012</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0907-4449</ISSN><JournalIssue CitedMedium="Print"><Volume>63</Volume><Issue>Pt 10</Issue><PubDate><Year>2007</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Biological crystallography</Title><ISOAbbreviation>Acta Crystallogr D Biol Crystallogr</ISOAbbreviation></Journal><ArticleTitle>Structure of sylvaticin, a new alpha-elicitin-like protein from Pythium sylvaticum.</ArticleTitle><Pagination><MedlinePgn>1102-8</MedlinePgn></Pagination><Abstract><AbstractText>The structure of sylvaticin, a 10 kDa major pythin protein excreted by the parasitic oomycete Pythium sylvaticum, has been determined. Although closely related to alpha-elicitins in its biological response, toxicity and overall structure, sylvaticin presents a number of structural features that make it an unusual member of the elicitin class. Elicitins possess a large hydrophobic cavity and the mechanism of the systemic acquired resistance induced in planta is known to proceed through lipid transport and complexation within this cavity. Unlike other elicitins, sylvaticin contains tryptophan residues, one of which points inwards towards the central cavity, thus limiting access to sterols. In the case of sylvaticin, the sterol-transport mechanism is likely to be of less importance compared with other members of the elicitin family and still remains to be fully characterized.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lascombe</LastName><ForeName>Marie-Bernard</ForeName><Initials>MB</Initials><AffiliationInfo><Affiliation>Laboratoire de Cristallographie et RMN Biologiques, Université Paris Descartes, UMR 8015 CNRS, Faculté de Pharmacie, 4 Avenue de l'Observatoire, 75006 Paris, France. marie-bernard.lascombe@univ-paris5.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Retailleau</LastName><ForeName>Pascal</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Ponchet</LastName><ForeName>Michel</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Industri</LastName><ForeName>Benoît</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Blein</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Prangé</LastName><ForeName>Thierry</ForeName><Initials>T</Initials></Author></AuthorList><Language>eng</Language><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>09</Month><Day>19</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 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Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011775" MajorTopicYN="N">Pythium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012997" MajorTopicYN="N">Solvents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013261" MajorTopicYN="N">Sterols</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2007</Year><Month>07</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2007</Year><Month>09</Month><Day>04</Day></PubMedPubDate><PubMedPubDate 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sortKey="Industri, Benoit" sort="Industri, Benoit" uniqKey="Industri B" first="Benoît" last="Industri">Benoît Industri</name><name sortKey="Ponchet, Michel" sort="Ponchet, Michel" uniqKey="Ponchet M" first="Michel" last="Ponchet">Michel Ponchet</name><name sortKey="Prange, Thierry" sort="Prange, Thierry" uniqKey="Prange T" first="Thierry" last="Prangé">Thierry Prangé</name><name sortKey="Retailleau, Pascal" sort="Retailleau, Pascal" uniqKey="Retailleau P" first="Pascal" last="Retailleau">Pascal Retailleau</name></noCountry><country name="France"><region name="Île-de-France"><name sortKey="Lascombe, Marie Bernard" sort="Lascombe, Marie Bernard" uniqKey="Lascombe M" first="Marie-Bernard" last="Lascombe">Marie-Bernard Lascombe</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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