Identification, characterization, and crystal structure of the Omega class glutathione transferases.
Identifieur interne : 001066 ( Main/Exploration ); précédent : 001065; suivant : 001067Identification, characterization, and crystal structure of the Omega class glutathione transferases.
Auteurs : P G Board [Australie] ; M. Coggan ; G. Chelvanayagam ; S. Easteal ; L S Jermiin ; G K Schulte ; D E Danley ; L R Hoth ; M C Griffor ; A V Kamath ; M H Rosner ; B A Chrunyk ; D E Perregaux ; C A Gabel ; K F Geoghegan ; J. PanditSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2000.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Caenorhabditis elegans (enzymologie), Cinétique (MeSH), Conformation des protéines (MeSH), Cristallographie aux rayons X (MeSH), Données de séquences moléculaires (MeSH), Femelle (MeSH), Glutathione transferase (composition chimique), Glutathione transferase (génétique), Glutathione transferase (métabolisme), Humains (MeSH), Isoenzymes (composition chimique), Isoenzymes (génétique), Isoenzymes (métabolisme), Mammifères (MeSH), Modèles moléculaires (MeSH), Mâle (MeSH), Phylogenèse (MeSH), Sites étiquetés par des séquences (MeSH), Spécificité du substrat (MeSH), Structure secondaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH), Transcription génétique (MeSH).
- MESH :
- composition chimique : Glutathione transferase, Isoenzymes.
- enzymologie : Caenorhabditis elegans.
- génétique : Glutathione transferase, Isoenzymes.
- métabolisme : Glutathione transferase, Isoenzymes.
- Animaux, Cinétique, Conformation des protéines, Cristallographie aux rayons X, Données de séquences moléculaires, Femelle, Humains, Mammifères, Modèles moléculaires, Mâle, Phylogenèse, Sites étiquetés par des séquences, Spécificité du substrat, Structure secondaire des protéines, Séquence d'acides aminés, Séquence nucléotidique, Transcription génétique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Base Sequence (MeSH), Caenorhabditis elegans (enzymology), Crystallography, X-Ray (MeSH), Female (MeSH), Glutathione Transferase (chemistry), Glutathione Transferase (genetics), Glutathione Transferase (metabolism), Humans (MeSH), Isoenzymes (chemistry), Isoenzymes (genetics), Isoenzymes (metabolism), Kinetics (MeSH), Male (MeSH), Mammals (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Phylogeny (MeSH), Protein Conformation (MeSH), Protein Structure, Secondary (MeSH), Sequence Tagged Sites (MeSH), Substrate Specificity (MeSH), Transcription, Genetic (MeSH).
- MESH :
- chemical , chemistry : Glutathione Transferase, Isoenzymes.
- enzymology : Caenorhabditis elegans.
- chemical , genetics : Glutathione Transferase, Isoenzymes.
- chemical , metabolism : Glutathione Transferase, Isoenzymes.
- Amino Acid Sequence, Animals, Base Sequence, Crystallography, X-Ray, Female, Humans, Kinetics, Male, Mammals, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Conformation, Protein Structure, Secondary, Sequence Tagged Sites, Substrate Specificity, Transcription, Genetic.
Abstract
A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment. Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans. In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins. The structure of GSTO 1-1 has been determined at 2.0-A resolution and has a characteristic GST fold (Protein Data Bank entry code ). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit. Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.
DOI: 10.1074/jbc.M001706200
PubMed: 10783391
Affiliations:
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Coggan</name></author><author><name sortKey="Chelvanayagam, G" sort="Chelvanayagam, G" uniqKey="Chelvanayagam G" first="G" last="Chelvanayagam">G. Chelvanayagam</name></author><author><name sortKey="Easteal, S" sort="Easteal, S" uniqKey="Easteal S" first="S" last="Easteal">S. Easteal</name></author><author><name sortKey="Jermiin, L S" sort="Jermiin, L S" uniqKey="Jermiin L" first="L S" last="Jermiin">L S Jermiin</name></author><author><name sortKey="Schulte, G K" sort="Schulte, G K" uniqKey="Schulte G" first="G K" last="Schulte">G K Schulte</name></author><author><name sortKey="Danley, D E" sort="Danley, D E" uniqKey="Danley D" first="D E" last="Danley">D E Danley</name></author><author><name sortKey="Hoth, L R" sort="Hoth, L R" uniqKey="Hoth L" first="L R" last="Hoth">L R Hoth</name></author><author><name sortKey="Griffor, M C" sort="Griffor, M C" uniqKey="Griffor M" first="M C" last="Griffor">M C Griffor</name></author><author><name sortKey="Kamath, A V" sort="Kamath, A V" uniqKey="Kamath A" first="A V" last="Kamath">A V Kamath</name></author><author><name sortKey="Rosner, M H" sort="Rosner, M H" uniqKey="Rosner M" first="M H" last="Rosner">M H Rosner</name></author><author><name sortKey="Chrunyk, B A" sort="Chrunyk, B A" uniqKey="Chrunyk B" first="B A" last="Chrunyk">B A Chrunyk</name></author><author><name sortKey="Perregaux, D E" sort="Perregaux, D E" uniqKey="Perregaux D" first="D E" last="Perregaux">D E Perregaux</name></author><author><name sortKey="Gabel, C A" sort="Gabel, C A" uniqKey="Gabel C" first="C A" last="Gabel">C A Gabel</name></author><author><name sortKey="Geoghegan, K F" sort="Geoghegan, K F" uniqKey="Geoghegan K" first="K F" last="Geoghegan">K F Geoghegan</name></author><author><name sortKey="Pandit, J" sort="Pandit, J" uniqKey="Pandit J" first="J" last="Pandit">J. Pandit</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2000" type="published">2000</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>Base Sequence (MeSH)</term><term>Caenorhabditis elegans (enzymology)</term><term>Crystallography, X-Ray (MeSH)</term><term>Female (MeSH)</term><term>Glutathione Transferase (chemistry)</term><term>Glutathione Transferase (genetics)</term><term>Glutathione Transferase (metabolism)</term><term>Humans (MeSH)</term><term>Isoenzymes (chemistry)</term><term>Isoenzymes (genetics)</term><term>Isoenzymes (metabolism)</term><term>Kinetics (MeSH)</term><term>Male (MeSH)</term><term>Mammals (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Phylogeny (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Protein Structure, Secondary (MeSH)</term><term>Sequence Tagged Sites (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Transcription, Genetic (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Caenorhabditis elegans (enzymologie)</term><term>Cinétique (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Femelle (MeSH)</term><term>Glutathione transferase (composition chimique)</term><term>Glutathione transferase (génétique)</term><term>Glutathione transferase (métabolisme)</term><term>Humains (MeSH)</term><term>Isoenzymes (composition chimique)</term><term>Isoenzymes (génétique)</term><term>Isoenzymes (métabolisme)</term><term>Mammifères (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Mâle (MeSH)</term><term>Phylogenèse (MeSH)</term><term>Sites étiquetés par des séquences (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Structure secondaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term><term>Transcription génétique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutathione Transferase</term><term>Isoenzymes</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutathione transferase</term><term>Isoenzymes</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Caenorhabditis elegans</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Caenorhabditis elegans</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutathione Transferase</term><term>Isoenzymes</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutathione transferase</term><term>Isoenzymes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione Transferase</term><term>Isoenzymes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathione transferase</term><term>Isoenzymes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Crystallography, X-Ray</term><term>Female</term><term>Humans</term><term>Kinetics</term><term>Male</term><term>Mammals</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Sequence Tagged Sites</term><term>Substrate Specificity</term><term>Transcription, Genetic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cinétique</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Femelle</term><term>Humains</term><term>Mammifères</term><term>Modèles moléculaires</term><term>Mâle</term><term>Phylogenèse</term><term>Sites étiquetés par des séquences</term><term>Spécificité du substrat</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Transcription génétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment. Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans. In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins. The structure of GSTO 1-1 has been determined at 2.0-A resolution and has a characteristic GST fold (Protein Data Bank entry code ). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit. Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10783391</PMID><DateCompleted><Year>2000</Year><Month>09</Month><Day>14</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>275</Volume><Issue>32</Issue><PubDate><Year>2000</Year><Month>Aug</Month><Day>11</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Identification, characterization, and crystal structure of the Omega class glutathione transferases.</ArticleTitle><Pagination><MedlinePgn>24798-806</MedlinePgn></Pagination><Abstract><AbstractText>A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment. Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans. In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins. The structure of GSTO 1-1 has been determined at 2.0-A resolution and has a characteristic GST fold (Protein Data Bank entry code ). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit. Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Board</LastName><ForeName>P G</ForeName><Initials>PG</Initials><AffiliationInfo><Affiliation>Molecular Genetics Group and Human Genetics Group, John Curtin School of Medical Research, Australian National University, Canberra, Australian Capital Territory 2601, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Coggan</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Chelvanayagam</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Easteal</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Jermiin</LastName><ForeName>L S</ForeName><Initials>LS</Initials></Author><Author ValidYN="Y"><LastName>Schulte</LastName><ForeName>G K</ForeName><Initials>GK</Initials></Author><Author ValidYN="Y"><LastName>Danley</LastName><ForeName>D E</ForeName><Initials>DE</Initials></Author><Author ValidYN="Y"><LastName>Hoth</LastName><ForeName>L R</ForeName><Initials>LR</Initials></Author><Author ValidYN="Y"><LastName>Griffor</LastName><ForeName>M C</ForeName><Initials>MC</Initials></Author><Author ValidYN="Y"><LastName>Kamath</LastName><ForeName>A V</ForeName><Initials>AV</Initials></Author><Author ValidYN="Y"><LastName>Rosner</LastName><ForeName>M H</ForeName><Initials>MH</Initials></Author><Author ValidYN="Y"><LastName>Chrunyk</LastName><ForeName>B A</ForeName><Initials>BA</Initials></Author><Author ValidYN="Y"><LastName>Perregaux</LastName><ForeName>D E</ForeName><Initials>DE</Initials></Author><Author ValidYN="Y"><LastName>Gabel</LastName><ForeName>C A</ForeName><Initials>CA</Initials></Author><Author ValidYN="Y"><LastName>Geoghegan</LastName><ForeName>K F</ForeName><Initials>KF</Initials></Author><Author ValidYN="Y"><LastName>Pandit</LastName><ForeName>J</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AF212303</AccessionNumber></AccessionNumberList></DataBank><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>1EEM</AccessionNumber></AccessionNumberList></DataBank></DataBankList><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>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber><NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CitationSubset>S</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017173" MajorTopicYN="N">Caenorhabditis elegans</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005982" MajorTopicYN="N">Glutathione Transferase</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="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008322" MajorTopicYN="N">Mammals</DescriptorName></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="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016324" MajorTopicYN="N">Sequence Tagged Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014158" MajorTopicYN="N">Transcription, Genetic</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>4</Month><Day>28</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2000</Year><Month>9</Month><Day>19</Day><Hour>11</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>4</Month><Day>28</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10783391</ArticleId><ArticleId IdType="doi">10.1074/jbc.M001706200</ArticleId><ArticleId IdType="pii">M001706200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li></country></list><tree><noCountry><name sortKey="Chelvanayagam, G" sort="Chelvanayagam, G" uniqKey="Chelvanayagam G" first="G" last="Chelvanayagam">G. Chelvanayagam</name><name sortKey="Chrunyk, B A" sort="Chrunyk, B A" uniqKey="Chrunyk B" first="B A" last="Chrunyk">B A Chrunyk</name><name sortKey="Coggan, M" sort="Coggan, M" uniqKey="Coggan M" first="M" last="Coggan">M. Coggan</name><name sortKey="Danley, D E" sort="Danley, D E" uniqKey="Danley D" first="D E" last="Danley">D E Danley</name><name sortKey="Easteal, S" sort="Easteal, S" uniqKey="Easteal S" first="S" last="Easteal">S. Easteal</name><name sortKey="Gabel, C A" sort="Gabel, C A" uniqKey="Gabel C" first="C A" last="Gabel">C A Gabel</name><name sortKey="Geoghegan, K F" sort="Geoghegan, K F" uniqKey="Geoghegan K" first="K F" last="Geoghegan">K F Geoghegan</name><name sortKey="Griffor, M C" sort="Griffor, M C" uniqKey="Griffor M" first="M C" last="Griffor">M C Griffor</name><name sortKey="Hoth, L R" sort="Hoth, L R" uniqKey="Hoth L" first="L R" last="Hoth">L R Hoth</name><name sortKey="Jermiin, L S" sort="Jermiin, L S" uniqKey="Jermiin L" first="L S" last="Jermiin">L S Jermiin</name><name sortKey="Kamath, A V" sort="Kamath, A V" uniqKey="Kamath A" first="A V" last="Kamath">A V Kamath</name><name sortKey="Pandit, J" sort="Pandit, J" uniqKey="Pandit J" first="J" last="Pandit">J. Pandit</name><name sortKey="Perregaux, D E" sort="Perregaux, D E" uniqKey="Perregaux D" first="D E" last="Perregaux">D E Perregaux</name><name sortKey="Rosner, M H" sort="Rosner, M H" uniqKey="Rosner M" first="M H" last="Rosner">M H Rosner</name><name sortKey="Schulte, G K" sort="Schulte, G K" uniqKey="Schulte G" first="G K" last="Schulte">G K Schulte</name></noCountry><country name="Australie"><noRegion><name sortKey="Board, P G" sort="Board, P G" uniqKey="Board P" first="P G" last="Board">P G Board</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|wiki= Bois
|area= GlutaredoxinV1
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|clé= pubmed:10783391
|texte= Identification, characterization, and crystal structure of the Omega class glutathione transferases.
}}
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