PhytophthoraV1, Main, Exploration, bibRecord, 002550

The 1.45 A resolution structure of the cryptogein-cholesterol complex: a close-up view of a sterol carrier protein (SCP) active site.

Identifieur interne : 002550 ( Main/Exploration ); précédent : 002549; suivant : 002551

The 1.45 A resolution structure of the cryptogein-cholesterol complex: a close-up view of a sterol carrier protein (SCP) active site.

Auteurs : Marie Bernard Lascombe [France] ; Michel Ponchet ; Paul Venard ; Marie Louise Milat ; Jean Pierre Blein ; Thierry Prangé

Source :

Acta crystallographica. Section D, Biological crystallography [ 0907-4449 ] ; 2002.

RBID : pubmed:12198300

Descripteurs français

English descriptors

KwdEn :
- Algal Proteins (chemistry), Amino Acid Sequence (MeSH), Binding Sites (MeSH), Carrier Proteins (chemistry), Carrier Proteins (metabolism), Cholesterol (chemistry), Fungal Proteins (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Molecular Structure (MeSH), Sequence Homology, Amino Acid (MeSH), Sterols (metabolism).
MESH :
- chemical , chemistry : Algal Proteins, Carrier Proteins, Cholesterol.
- chemical , metabolism : Carrier Proteins, Sterols.
- Amino Acid Sequence, Binding Sites, Fungal Proteins, Models, Molecular, Molecular Sequence Data, Molecular Structure, Sequence Homology, Amino Acid.

Abstract

Cryptogein is a small 10 kDa elicitor produced by the phytoparasitic oomycete Phytophthora cryptogea. The protein also displays a sterol carrier activity. The native protein crystallizes in space group P4(1)22, with unit-cell parameters a = b = 46.51, c = 134.9 A (diffraction limit: 2.1 A). Its complex with cholesterol crystallizes in space group C222(1), with unit-cell parameters a = 30.96, b = 94.8, c = 65.3 A and a resolution enhanced to 1.45 A. The large inner non-specific hydrophobic cavity is able to accommodate a large variety of 3-beta-hydroxy sterols. Cryptogein probably acts as a sterol shuttle helping the pathogen to grow and complete its life cycle.

DOI: 10.1107/S0907444902011745
PubMed: 12198300

Affiliations:

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Le document en format XML

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<author><name sortKey="Venard, Paul" sort="Venard, Paul" uniqKey="Venard P" first="Paul" last="Venard">Paul Venard</name>
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<author><name sortKey="Milat, Marie Louise" sort="Milat, Marie Louise" uniqKey="Milat M" first="Marie Louise" last="Milat">Marie Louise Milat</name>
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<author><name sortKey="Blein, Jean Pierre" sort="Blein, Jean Pierre" uniqKey="Blein J" first="Jean Pierre" last="Blein">Jean Pierre Blein</name>
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<term>Amino Acid Sequence (MeSH)</term>
<term>Binding Sites (MeSH)</term>
<term>Carrier Proteins (chemistry)</term>
<term>Carrier Proteins (metabolism)</term>
<term>Cholesterol (chemistry)</term>
<term>Fungal Proteins (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Molecular Structure (MeSH)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Sterols (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Cholestérol (composition chimique)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Protéines d'algue (composition chimique)</term>
<term>Protéines de transport (composition chimique)</term>
<term>Protéines de transport (métabolisme)</term>
<term>Protéines fongiques (MeSH)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Sites de fixation (MeSH)</term>
<term>Structure moléculaire (MeSH)</term>
<term>Stérols (métabolisme)</term>
<term>Séquence d'acides aminés (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Algal Proteins</term>
<term>Carrier Proteins</term>
<term>Cholesterol</term>
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<term>Sterols</term>
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<term>Protéines d'algue</term>
<term>Protéines de transport</term>
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<term>Stérols</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Binding Sites</term>
<term>Fungal Proteins</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Molecular Structure</term>
<term>Sequence Homology, Amino Acid</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term>
<term>Modèles moléculaires</term>
<term>Protéines fongiques</term>
<term>Similitude de séquences d'acides aminés</term>
<term>Sites de fixation</term>
<term>Structure moléculaire</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Cryptogein is a small 10 kDa elicitor produced by the phytoparasitic oomycete Phytophthora cryptogea. The protein also displays a sterol carrier activity. The native protein crystallizes in space group P4(1)22, with unit-cell parameters a = b = 46.51, c = 134.9 A (diffraction limit: 2.1 A). Its complex with cholesterol crystallizes in space group C222(1), with unit-cell parameters a = 30.96, b = 94.8, c = 65.3 A and a resolution enhanced to 1.45 A. The large inner non-specific hydrophobic cavity is able to accommodate a large variety of 3-beta-hydroxy sterols. Cryptogein probably acts as a sterol shuttle helping the pathogen to grow and complete its life cycle.</div>
</front>
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<DateCompleted><Year>2003</Year>
<Month>02</Month>
<Day>13</Day>
</DateCompleted>
<DateRevised><Year>2013</Year>
<Month>11</Month>
<Day>21</Day>
</DateRevised>
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<Title>Acta crystallographica. Section D, Biological crystallography</Title>
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<ArticleTitle>The 1.45 A resolution structure of the cryptogein-cholesterol complex: a close-up view of a sterol carrier protein (SCP) active site.</ArticleTitle>
<Pagination><MedlinePgn>1442-7</MedlinePgn>
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<Abstract><AbstractText>Cryptogein is a small 10 kDa elicitor produced by the phytoparasitic oomycete Phytophthora cryptogea. The protein also displays a sterol carrier activity. The native protein crystallizes in space group P4(1)22, with unit-cell parameters a = b = 46.51, c = 134.9 A (diffraction limit: 2.1 A). Its complex with cholesterol crystallizes in space group C222(1), with unit-cell parameters a = 30.96, b = 94.8, c = 65.3 A and a resolution enhanced to 1.45 A. The large inner non-specific hydrophobic cavity is able to accommodate a large variety of 3-beta-hydroxy sterols. Cryptogein probably acts as a sterol shuttle helping the pathogen to grow and complete its life cycle.</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 (UMR-8015, CNRS), Faculté de Pharmacie, 4 Avenue de l'Observatoire, 75270 Paris CEDEX 06, France. lascombe@pharmacie.univ-paris5.fr</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ponchet</LastName>
<ForeName>Michel</ForeName>
<Initials>M</Initials>
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<Author ValidYN="Y"><LastName>Venard</LastName>
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<ForeName>Marie Louise</ForeName>
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<Author ValidYN="Y"><LastName>Blein</LastName>
<ForeName>Jean Pierre</ForeName>
<Initials>JP</Initials>
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<Author ValidYN="Y"><LastName>Prangé</LastName>
<ForeName>Thierry</ForeName>
<Initials>T</Initials>
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The 1.45 A resolution structure of the cryptogein-cholesterol complex: a close-up view of a sterol carrier protein (SCP) active site.

The 1.45 A resolution structure of the cryptogein-cholesterol complex: a close-up view of a sterol carrier protein (SCP) active site.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki