Crystal structure of the glutaredoxin-like protein SH3BGRL3 at 1.6 Angstrom resolution.
Identifieur interne : 000E88 ( Main/Exploration ); précédent : 000E87; suivant : 000E89Crystal structure of the glutaredoxin-like protein SH3BGRL3 at 1.6 Angstrom resolution.
Auteurs : Marco Nardini [Italie] ; Michela Mazzocco ; Anna Massaro ; Massimo Maffei ; Alessandro Vergano ; Alessandra Donadini ; Paolo Scartezzini ; Martino BolognesiSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2004.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Animaux (MeSH), Conformation des protéines (MeSH), Cristallographie aux rayons X (MeSH), Données de séquences moléculaires (MeSH), Escherichia coli (métabolisme), Glutarédoxines (MeSH), Modèles moléculaires (MeSH), Oxidoreductases (MeSH), Protéines (composition chimique), Protéines (génétique), Protéines de fusion recombinantes (composition chimique), Protéines de fusion recombinantes (génétique), Protéines de transport (composition chimique), Protéines de transport (génétique), Résonance magnétique nucléaire biomoléculaire (MeSH), Souris (MeSH), Séquence d'acides aminés (MeSH), Électricité statique (MeSH).
- MESH :
- composition chimique : Protéines, Protéines de fusion recombinantes, Protéines de transport.
- génétique : Protéines, Protéines de fusion recombinantes, Protéines de transport.
- métabolisme : Escherichia coli.
- Alignement de séquences, Animaux, Conformation des protéines, Cristallographie aux rayons X, Données de séquences moléculaires, Glutarédoxines, Modèles moléculaires, Oxidoreductases, Résonance magnétique nucléaire biomoléculaire, Souris, Séquence d'acides aminés, Électricité statique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Carrier Proteins (chemistry), Carrier Proteins (genetics), Crystallography, X-Ray (MeSH), Escherichia coli (metabolism), Glutaredoxins (MeSH), Mice (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Nuclear Magnetic Resonance, Biomolecular (MeSH), Oxidoreductases (MeSH), Protein Conformation (MeSH), Proteins (chemistry), Proteins (genetics), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Sequence Alignment (MeSH), Static Electricity (MeSH).
- MESH :
- chemical , chemistry : Carrier Proteins, Proteins, Recombinant Fusion Proteins.
- chemical , genetics : Carrier Proteins, Proteins, Recombinant Fusion Proteins.
- metabolism : Escherichia coli.
- Amino Acid Sequence, Animals, Crystallography, X-Ray, Glutaredoxins, Mice, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Oxidoreductases, Protein Conformation, Sequence Alignment, Static Electricity.
Abstract
We report the 1.6 Angstrom resolution crystal structure of SH3BGRL3, a member of a new mammalian protein family of unknown function. The observed "thioredoxin fold" of SH3BGRL3 matches the tertiary structure of glutaredoxins, even in the N-terminal region where the sequence similarity between the two protein families is negligible. In particular, SH3BGRL3 displays structural modifications at the N-terminal Cys-x-x-Cys loop, responsible for glutathione binding and catalysis in glutaredoxins. The loop hosts a six residue insertion, yielding an extra N-terminal-capped helical turn, first observed here for the thioredoxin fold. This, together with deletion of both Cys residues, results in a substantial reshaping of the neighboring cleft, where glutathione is hosted in glutaredoxins. While not active in redox reaction and glutathione binding, SH3BGRL3 may act as an endogenous modulator of glutaredoxin activities by competing, with its fully conserved thioredoxin fold, for binding to yet unknown target proteins.
DOI: 10.1016/j.bbrc.2004.04.050
PubMed: 15120624
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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first="Anna" last="Massaro">Anna Massaro</name></author><author><name sortKey="Maffei, Massimo" sort="Maffei, Massimo" uniqKey="Maffei M" first="Massimo" last="Maffei">Massimo Maffei</name></author><author><name sortKey="Vergano, Alessandro" sort="Vergano, Alessandro" uniqKey="Vergano A" first="Alessandro" last="Vergano">Alessandro Vergano</name></author><author><name sortKey="Donadini, Alessandra" sort="Donadini, Alessandra" uniqKey="Donadini A" first="Alessandra" last="Donadini">Alessandra Donadini</name></author><author><name sortKey="Scartezzini, Paolo" sort="Scartezzini, Paolo" uniqKey="Scartezzini P" first="Paolo" last="Scartezzini">Paolo Scartezzini</name></author><author><name sortKey="Bolognesi, Martino" sort="Bolognesi, Martino" uniqKey="Bolognesi M" first="Martino" last="Bolognesi">Martino Bolognesi</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2004">2004</date><idno type="RBID">pubmed:15120624</idno><idno 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Fisica-INFM e Centro di Eccellenza per la Ricerca Biomedica, Università di Genova, Via Dodecaneso 33, 16146 Genoa</wicri:regionArea><wicri:noRegion>16146 Genoa</wicri:noRegion></affiliation></author><author><name sortKey="Mazzocco, Michela" sort="Mazzocco, Michela" uniqKey="Mazzocco M" first="Michela" last="Mazzocco">Michela Mazzocco</name></author><author><name sortKey="Massaro, Anna" sort="Massaro, Anna" uniqKey="Massaro A" first="Anna" last="Massaro">Anna Massaro</name></author><author><name sortKey="Maffei, Massimo" sort="Maffei, Massimo" uniqKey="Maffei M" first="Massimo" last="Maffei">Massimo Maffei</name></author><author><name sortKey="Vergano, Alessandro" sort="Vergano, Alessandro" uniqKey="Vergano A" first="Alessandro" last="Vergano">Alessandro Vergano</name></author><author><name sortKey="Donadini, Alessandra" sort="Donadini, Alessandra" uniqKey="Donadini A" first="Alessandra" last="Donadini">Alessandra Donadini</name></author><author><name sortKey="Scartezzini, Paolo" sort="Scartezzini, Paolo" uniqKey="Scartezzini P" first="Paolo" last="Scartezzini">Paolo Scartezzini</name></author><author><name sortKey="Bolognesi, Martino" sort="Bolognesi, Martino" uniqKey="Bolognesi M" first="Martino" last="Bolognesi">Martino Bolognesi</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Carrier Proteins (chemistry)</term><term>Carrier Proteins (genetics)</term><term>Crystallography, X-Ray (MeSH)</term><term>Escherichia coli (metabolism)</term><term>Glutaredoxins (MeSH)</term><term>Mice (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Nuclear Magnetic Resonance, Biomolecular (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Proteins (chemistry)</term><term>Proteins (genetics)</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Sequence Alignment (MeSH)</term><term>Static Electricity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Animaux (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Protéines (composition chimique)</term><term>Protéines (génétique)</term><term>Protéines de fusion recombinantes (composition chimique)</term><term>Protéines de fusion recombinantes (génétique)</term><term>Protéines de transport (composition chimique)</term><term>Protéines de transport (génétique)</term><term>Résonance magnétique nucléaire biomoléculaire (MeSH)</term><term>Souris (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Électricité statique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carrier Proteins</term><term>Proteins</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Carrier Proteins</term><term>Proteins</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines</term><term>Protéines de fusion recombinantes</term><term>Protéines de transport</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines</term><term>Protéines de fusion recombinantes</term><term>Protéines de transport</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Escherichia coli</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Crystallography, X-Ray</term><term>Glutaredoxins</term><term>Mice</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Oxidoreductases</term><term>Protein Conformation</term><term>Sequence Alignment</term><term>Static Electricity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Modèles moléculaires</term><term>Oxidoreductases</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Souris</term><term>Séquence d'acides aminés</term><term>Électricité statique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We report the 1.6 Angstrom resolution crystal structure of SH3BGRL3, a member of a new mammalian protein family of unknown function. The observed "thioredoxin fold" of SH3BGRL3 matches the tertiary structure of glutaredoxins, even in the N-terminal region where the sequence similarity between the two protein families is negligible. In particular, SH3BGRL3 displays structural modifications at the N-terminal Cys-x-x-Cys loop, responsible for glutathione binding and catalysis in glutaredoxins. The loop hosts a six residue insertion, yielding an extra N-terminal-capped helical turn, first observed here for the thioredoxin fold. This, together with deletion of both Cys residues, results in a substantial reshaping of the neighboring cleft, where glutathione is hosted in glutaredoxins. While not active in redox reaction and glutathione binding, SH3BGRL3 may act as an endogenous modulator of glutaredoxin activities by competing, with its fully conserved thioredoxin fold, for binding to yet unknown target proteins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15120624</PMID><DateCompleted><Year>2004</Year><Month>06</Month><Day>25</Day></DateCompleted><DateRevised><Year>2008</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>318</Volume><Issue>2</Issue><PubDate><Year>2004</Year><Month>May</Month><Day>28</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Crystal structure of the glutaredoxin-like protein SH3BGRL3 at 1.6 Angstrom resolution.</ArticleTitle><Pagination><MedlinePgn>470-6</MedlinePgn></Pagination><Abstract><AbstractText>We report the 1.6 Angstrom resolution crystal structure of SH3BGRL3, a member of a new mammalian protein family of unknown function. The observed "thioredoxin fold" of SH3BGRL3 matches the tertiary structure of glutaredoxins, even in the N-terminal region where the sequence similarity between the two protein families is negligible. In particular, SH3BGRL3 displays structural modifications at the N-terminal Cys-x-x-Cys loop, responsible for glutathione binding and catalysis in glutaredoxins. The loop hosts a six residue insertion, yielding an extra N-terminal-capped helical turn, first observed here for the thioredoxin fold. This, together with deletion of both Cys residues, results in a substantial reshaping of the neighboring cleft, where glutathione is hosted in glutaredoxins. While not active in redox reaction and glutathione binding, SH3BGRL3 may act as an endogenous modulator of glutaredoxin activities by competing, with its fully conserved thioredoxin fold, for binding to yet unknown target proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nardini</LastName><ForeName>Marco</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Dipartimento di Fisica-INFM e Centro di Eccellenza per la Ricerca Biomedica, Università di Genova, Via Dodecaneso 33, 16146 Genoa, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mazzocco</LastName><ForeName>Michela</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Massaro</LastName><ForeName>Anna</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Maffei</LastName><ForeName>Massimo</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Vergano</LastName><ForeName>Alessandro</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Donadini</LastName><ForeName>Alessandra</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Scartezzini</LastName><ForeName>Paolo</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Bolognesi</LastName><ForeName>Martino</ForeName><Initials>M</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></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier 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Biomolecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055672" MajorTopicYN="N">Static Electricity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2004</Year><Month>04</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>5</Month><Day>4</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>6</Month><Day>26</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>5</Month><Day>4</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15120624</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2004.04.050</ArticleId><ArticleId IdType="pii">S0006291X04007739</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li></country></list><tree><noCountry><name sortKey="Bolognesi, Martino" sort="Bolognesi, Martino" uniqKey="Bolognesi M" first="Martino" last="Bolognesi">Martino Bolognesi</name><name sortKey="Donadini, Alessandra" sort="Donadini, Alessandra" uniqKey="Donadini A" first="Alessandra" last="Donadini">Alessandra Donadini</name><name sortKey="Maffei, Massimo" sort="Maffei, Massimo" uniqKey="Maffei M" first="Massimo" last="Maffei">Massimo Maffei</name><name sortKey="Massaro, Anna" sort="Massaro, Anna" uniqKey="Massaro A" first="Anna" last="Massaro">Anna Massaro</name><name sortKey="Mazzocco, Michela" sort="Mazzocco, Michela" uniqKey="Mazzocco M" first="Michela" last="Mazzocco">Michela Mazzocco</name><name sortKey="Scartezzini, Paolo" sort="Scartezzini, Paolo" uniqKey="Scartezzini P" first="Paolo" last="Scartezzini">Paolo Scartezzini</name><name sortKey="Vergano, Alessandro" sort="Vergano, Alessandro" uniqKey="Vergano A" first="Alessandro" last="Vergano">Alessandro Vergano</name></noCountry><country name="Italie"><noRegion><name sortKey="Nardini, Marco" sort="Nardini, Marco" uniqKey="Nardini M" first="Marco" last="Nardini">Marco Nardini</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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