ThaumatinV1, Main, Corpus, bibRecord, 000457

Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices.

Identifieur interne : 000457 ( Main/Corpus ); précédent : 000456; suivant : 000458

Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices.

Auteurs : Christophe Charron ; Richard Giegé ; Bernard Lorber

Source :

Acta crystallographica. Section D, Biological crystallography [ 0907-4449 ] ; 2004.

RBID : pubmed:14684896

English descriptors

KwdEn :
- Crystallization (MeSH), Crystallography, X-Ray (MeSH), Hydrogen Bonding (MeSH), Models, Molecular (MeSH), Plant Proteins (chemistry).
MESH :
- chemical , chemistry : Plant Proteins.
- Crystallization, Crystallography, X-Ray, Hydrogen Bonding, Models, Molecular.

Abstract

The intensely sweet protein thaumatin has been crystallized in a hexagonal lattice after a temperature shift from 293 to 277 K. The structure of the protein in the new crystal was solved at 1.6 A resolution. The protein fold is identical to that found in three other crystal forms grown in the presence of crystallizing agents of differing chemical natures. The proportions of lattice interactions involving hydrogen bonds, hydrophobic or ionic groups differ greatly from one form to another. Moreover, the distribution of acidic and basic residues taking part in contacts also varies. The hexagonal packing is characterized by the presence of channels parallel to the c axis that are so wide that protein molecules can diffuse through them.

DOI: 10.1107/s0907444903022613
PubMed: 14684896

Links to Exploration step

pubmed:14684896

Le document en format XML

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<author><name sortKey="Charron, Christophe" sort="Charron, Christophe" uniqKey="Charron C" first="Christophe" last="Charron">Christophe Charron</name>
<affiliation><nlm:affiliation>Département 'Mécanismes et Macromolécules de la Synthèse Protéique et Cristallogenèse' UPR 9002, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15Rue René Descartes, F-67084 Strasbourg CEDEX, France.</nlm:affiliation>
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<author><name sortKey="Giege, Richard" sort="Giege, Richard" uniqKey="Giege R" first="Richard" last="Giegé">Richard Giegé</name>
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<author><name sortKey="Lorber, Bernard" sort="Lorber, Bernard" uniqKey="Lorber B" first="Bernard" last="Lorber">Bernard Lorber</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices.</title>
<author><name sortKey="Charron, Christophe" sort="Charron, Christophe" uniqKey="Charron C" first="Christophe" last="Charron">Christophe Charron</name>
<affiliation><nlm:affiliation>Département 'Mécanismes et Macromolécules de la Synthèse Protéique et Cristallogenèse' UPR 9002, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15Rue René Descartes, F-67084 Strasbourg CEDEX, France.</nlm:affiliation>
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<author><name sortKey="Giege, Richard" sort="Giege, Richard" uniqKey="Giege R" first="Richard" last="Giegé">Richard Giegé</name>
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<author><name sortKey="Lorber, Bernard" sort="Lorber, Bernard" uniqKey="Lorber B" first="Bernard" last="Lorber">Bernard Lorber</name>
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<series><title level="j">Acta crystallographica. Section D, Biological crystallography</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Crystallization (MeSH)</term>
<term>Crystallography, X-Ray (MeSH)</term>
<term>Hydrogen Bonding (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Plant Proteins (chemistry)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Plant Proteins</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Crystallization</term>
<term>Crystallography, X-Ray</term>
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<front><div type="abstract" xml:lang="en">The intensely sweet protein thaumatin has been crystallized in a hexagonal lattice after a temperature shift from 293 to 277 K. The structure of the protein in the new crystal was solved at 1.6 A resolution. The protein fold is identical to that found in three other crystal forms grown in the presence of crystallizing agents of differing chemical natures. The proportions of lattice interactions involving hydrogen bonds, hydrophobic or ionic groups differ greatly from one form to another. Moreover, the distribution of acidic and basic residues taking part in contacts also varies. The hexagonal packing is characterized by the presence of channels parallel to the c axis that are so wide that protein molecules can diffuse through them.</div>
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<DateRevised><Year>2019</Year>
<Month>06</Month>
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<JournalIssue CitedMedium="Print"><Volume>60</Volume>
<Issue>Pt 1</Issue>
<PubDate><Year>2004</Year>
<Month>Jan</Month>
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<Title>Acta crystallographica. Section D, Biological crystallography</Title>
<ISOAbbreviation>Acta Crystallogr D Biol Crystallogr</ISOAbbreviation>
</Journal>
<ArticleTitle>Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices.</ArticleTitle>
<Pagination><MedlinePgn>83-9</MedlinePgn>
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<Abstract><AbstractText>The intensely sweet protein thaumatin has been crystallized in a hexagonal lattice after a temperature shift from 293 to 277 K. The structure of the protein in the new crystal was solved at 1.6 A resolution. The protein fold is identical to that found in three other crystal forms grown in the presence of crystallizing agents of differing chemical natures. The proportions of lattice interactions involving hydrogen bonds, hydrophobic or ionic groups differ greatly from one form to another. Moreover, the distribution of acidic and basic residues taking part in contacts also varies. The hexagonal packing is characterized by the presence of channels parallel to the c axis that are so wide that protein molecules can diffuse through them.</AbstractText>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Charron</LastName>
<ForeName>Christophe</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Département 'Mécanismes et Macromolécules de la Synthèse Protéique et Cristallogenèse' UPR 9002, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15Rue René Descartes, F-67084 Strasbourg CEDEX, France.</Affiliation>
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<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType>
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<Month>12</Month>
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<Chemical><RegistryNumber>53850-34-3</RegistryNumber>
<NameOfSubstance UI="C003427">thaumatin protein, plant</NameOfSubstance>
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Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices.

Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices.

Source :

English descriptors

Abstract

Links to Exploration step

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