A possible binding path of ergosterol within elicitins revealed by molecular dynamics.
Identifieur interne : 002865 ( Main/Exploration ); précédent : 002864; suivant : 002866A possible binding path of ergosterol within elicitins revealed by molecular dynamics.
Auteurs : S. Demaret [France] ; J P Demaret ; S. BrunieSource :
- Journal of biomolecular structure & dynamics [ 0739-1102 ] ; 2000.
Descripteurs français
- KwdFr :
- Conformation des protéines (MeSH), Données de séquences moléculaires (MeSH), Ergostérol (composition chimique), Ergostérol (métabolisme), Modèles moléculaires (MeSH), Mutation (MeSH), Phytophthora (composition chimique), Phytophthora (génétique), Protéines d'algue (MeSH), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Sites de fixation (MeSH), Séquence d'acides aminés (MeSH), Thermodynamique (MeSH).
- MESH :
- composition chimique : Ergostérol, Phytophthora, Protéines fongiques.
- génétique : Phytophthora, Protéines fongiques.
- métabolisme : Ergostérol, Protéines fongiques.
- Conformation des protéines, Données de séquences moléculaires, Modèles moléculaires, Mutation, Protéines d'algue, Sites de fixation, Séquence d'acides aminés, Thermodynamique.
English descriptors
- KwdEn :
- Algal Proteins (MeSH), Amino Acid Sequence (MeSH), Binding Sites (MeSH), Ergosterol (chemistry), Ergosterol (metabolism), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Mutation (MeSH), Phytophthora (chemistry), Phytophthora (genetics), Protein Conformation (MeSH), Thermodynamics (MeSH).
- MESH :
- chemical , chemistry : Ergosterol, Fungal Proteins.
- chemical , genetics : Fungal Proteins.
- chemical , metabolism : Ergosterol, Fungal Proteins.
- chemical : Algal Proteins.
- chemistry : Phytophthora.
- genetics : Phytophthora.
- Amino Acid Sequence, Binding Sites, Models, Molecular, Molecular Sequence Data, Mutation, Protein Conformation, Thermodynamics.
Abstract
Elicitins, produced by most of the phytopathogenic fungi of the genus Phytophthora, provoke in the tobacco plant both remote leaf necrosis and the induction of a resistance against subsequent attack by various micro-organisms. The crystal structure of b-cryptogein (CRY), secreted by Phytophthora cryptogea, was previously reported as well as the first structure of a SCP/sterol complex, the ergosterol-complexed, mutated CRY (K13H). In K13H, the ergosterol molecule is encapsulated in a large internal hydrophobic cavity which is not present in CRY. This binding induces a minor conformational change in the protein structure. Molecular dynamics studies were undertaken to precise the structural behaviour of CRY and K13H with respect to the complexation of the ergosterol. Although it is not possible to simulate the entrance of the ergosterol in the protein, we assume that capture and release of the ligand possibly both occur following the same path. Our results show that, in the complex K13H, the ergosterol molecule is pushed towards the residue 13 which play a key role in the necrotic activity of the protein. It is likely that the polarity of residue 13, favouring the binding of the hydroxyl of the ligand, would be involved in the recognition of the sterol and in an optimisation of its orientation. Thus, in a first step, the molecule of ergosterol would be rotated around itself to a position which makes possible, in a second step, its translation to the internal cavity, as a key in a keyhole.
DOI: 10.1080/07391102.2000.10506680
PubMed: 11149520
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Brunie</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2000">2000</date><idno type="RBID">pubmed:11149520</idno><idno type="pmid">11149520</idno><idno type="doi">10.1080/07391102.2000.10506680</idno><idno type="wicri:Area/Main/Corpus">002813</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002813</idno><idno type="wicri:Area/Main/Curation">002813</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002813</idno><idno type="wicri:Area/Main/Exploration">002813</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A possible binding path of ergosterol within elicitins revealed by molecular dynamics.</title><author><name sortKey="Demaret, S" sort="Demaret, S" uniqKey="Demaret S" first="S" last="Demaret">S. Demaret</name><affiliation wicri:level="3"><nlm:affiliation>CBM-CNRS, Orléans, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>CBM-CNRS, Orléans</wicri:regionArea><placeName><region type="region">Centre-Val de Loire</region><region type="old region">Région Centre</region><settlement type="city">Orléans</settlement></placeName></affiliation></author><author><name sortKey="Demaret, J P" sort="Demaret, J P" uniqKey="Demaret J" first="J P" last="Demaret">J P Demaret</name></author><author><name sortKey="Brunie, S" sort="Brunie, S" uniqKey="Brunie S" first="S" last="Brunie">S. 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The crystal structure of b-cryptogein (CRY), secreted by Phytophthora cryptogea, was previously reported as well as the first structure of a SCP/sterol complex, the ergosterol-complexed, mutated CRY (K13H). In K13H, the ergosterol molecule is encapsulated in a large internal hydrophobic cavity which is not present in CRY. This binding induces a minor conformational change in the protein structure. Molecular dynamics studies were undertaken to precise the structural behaviour of CRY and K13H with respect to the complexation of the ergosterol. Although it is not possible to simulate the entrance of the ergosterol in the protein, we assume that capture and release of the ligand possibly both occur following the same path. Our results show that, in the complex K13H, the ergosterol molecule is pushed towards the residue 13 which play a key role in the necrotic activity of the protein. It is likely that the polarity of residue 13, favouring the binding of the hydroxyl of the ligand, would be involved in the recognition of the sterol and in an optimisation of its orientation. Thus, in a first step, the molecule of ergosterol would be rotated around itself to a position which makes possible, in a second step, its translation to the internal cavity, as a key in a keyhole.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11149520</PMID><DateCompleted><Year>2001</Year><Month>03</Month><Day>22</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0739-1102</ISSN><JournalIssue CitedMedium="Print"><Volume>18</Volume><Issue>3</Issue><PubDate><Year>2000</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Journal of biomolecular structure & dynamics</Title><ISOAbbreviation>J Biomol Struct Dyn</ISOAbbreviation></Journal><ArticleTitle>A possible binding path of ergosterol within elicitins revealed by molecular dynamics.</ArticleTitle><Pagination><MedlinePgn>453-60</MedlinePgn></Pagination><Abstract><AbstractText>Elicitins, produced by most of the phytopathogenic fungi of the genus Phytophthora, provoke in the tobacco plant both remote leaf necrosis and the induction of a resistance against subsequent attack by various micro-organisms. The crystal structure of b-cryptogein (CRY), secreted by Phytophthora cryptogea, was previously reported as well as the first structure of a SCP/sterol complex, the ergosterol-complexed, mutated CRY (K13H). In K13H, the ergosterol molecule is encapsulated in a large internal hydrophobic cavity which is not present in CRY. This binding induces a minor conformational change in the protein structure. Molecular dynamics studies were undertaken to precise the structural behaviour of CRY and K13H with respect to the complexation of the ergosterol. Although it is not possible to simulate the entrance of the ergosterol in the protein, we assume that capture and release of the ligand possibly both occur following the same path. Our results show that, in the complex K13H, the ergosterol molecule is pushed towards the residue 13 which play a key role in the necrotic activity of the protein. It is likely that the polarity of residue 13, favouring the binding of the hydroxyl of the ligand, would be involved in the recognition of the sterol and in an optimisation of its orientation. Thus, in a first step, the molecule of ergosterol would be rotated around itself to a position which makes possible, in a second step, its translation to the internal cavity, as a key in a keyhole.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Demaret</LastName><ForeName>S</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>CBM-CNRS, Orléans, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Demaret</LastName><ForeName>J P</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Brunie</LastName><ForeName>S</ForeName><Initials>S</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Biomol Struct Dyn</MedlineTA><NlmUniqueID>8404176</NlmUniqueID><ISSNLinking>0739-1102</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="C061032">cryptogein protein, Phytophthora cryptogea</NameOfSubstance></Chemical><Chemical><RegistryNumber>Z30RAY509F</RegistryNumber><NameOfSubstance UI="D004875">Ergosterol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020418" MajorTopicYN="Y">Algal Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004875" MajorTopicYN="N">Ergosterol</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></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="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010838" MajorTopicYN="N">Phytophthora</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year><Month>1</Month><Day>10</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>3</Month><Day>27</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2001</Year><Month>1</Month><Day>10</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11149520</ArticleId><ArticleId IdType="doi">10.1080/07391102.2000.10506680</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Centre-Val de Loire</li><li>Région Centre</li></region><settlement><li>Orléans</li></settlement></list><tree><noCountry><name sortKey="Brunie, S" sort="Brunie, S" uniqKey="Brunie S" first="S" last="Brunie">S. Brunie</name><name sortKey="Demaret, J P" sort="Demaret, J P" uniqKey="Demaret J" first="J P" last="Demaret">J P Demaret</name></noCountry><country name="France"><region name="Centre-Val de Loire"><name sortKey="Demaret, S" sort="Demaret, S" uniqKey="Demaret S" first="S" last="Demaret">S. Demaret</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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