Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysis.
Identifieur interne : 001204 ( Main/Exploration ); précédent : 001203; suivant : 001205Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysis.
Auteurs : F. Aslund [Suède] ; K. Nordstrand ; K D Berndt ; M. Nikkola ; T. Bergman ; H. Ponstingl ; H. Jörnvall ; G. Otting ; A. HolmgrenSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1996.
Descripteurs français
- KwdFr :
- Conformation des protéines (MeSH), Disulfures (métabolisme), Données de séquences moléculaires (MeSH), Escherichia coli (composition chimique), Glutarédoxines (MeSH), Isotopes de l'azote (MeSH), Modèles moléculaires (MeSH), Oxidoreductases (MeSH), Protons (MeSH), Protéines (composition chimique), Protéines (métabolisme), Similitude de séquences d'acides aminés (MeSH), Spectroscopie par résonance magnétique (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Escherichia coli, Protéines.
- métabolisme : Disulfures, Protéines.
- Conformation des protéines, Données de séquences moléculaires, Glutarédoxines, Isotopes de l'azote, Modèles moléculaires, Oxidoreductases, Protons, Similitude de séquences d'acides aminés, Spectroscopie par résonance magnétique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Disulfides (metabolism), Escherichia coli (chemistry), Glutaredoxins (MeSH), Magnetic Resonance Spectroscopy (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Nitrogen Isotopes (MeSH), Oxidoreductases (MeSH), Protein Conformation (MeSH), Proteins (chemistry), Proteins (metabolism), Protons (MeSH), Sequence Homology, Amino Acid (MeSH).
- MESH :
- chemical , chemistry : Proteins.
- chemical , metabolism : Disulfides, Proteins.
- chemistry : Escherichia coli.
- Amino Acid Sequence, Glutaredoxins, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Nitrogen Isotopes, Oxidoreductases, Protein Conformation, Protons, Sequence Homology, Amino Acid.
Abstract
The primary and secondary structure of glutaredoxin-3 (Grx3), a glutathione-disulfide oxidoreductase from Escherichia coli, has been determined. The amino acid sequence of Grx3 consists of 82 residues and contains a redox-active motif, Cys-Pro-Tyr-Cys, typical of the glutaredoxin family. Sequence comparison reveals a homology (33% identity) to that of glutaredoxin-1 (Grx1) from E. coli as well as to other members of the thioredoxin superfamily. In addition to the active site cysteine residues, Grx3 contains one additional cysteine (Cys65) corresponding to one of the two non-active site (or structural) cysteine residues present in mammalian glutaredoxins. The sequence-specific 1H and 15N nuclear magnetic resonance assignments of reduced Grx3 have been obtained. From a combined analysis of chemical shifts, 3JHNalpha coupling constants, sequential and medium range NOEs, and amide proton exchange rates, the secondary structure of reduced Grx3 was determined and found to be very similar to that inferred from amino acid sequence comparison to homologous proteins. The consequences of the proposed structural similarity to Grx1 are that Grx3, while possessing a largely intact GSH binding cleft, would have a very different spatial distribution of charged residues, most notably surrounding the active site cysteine residues and occurring in the proposed hydrophobic protein-protein interaction area. These differences may contribute to the observed very low Kcat of Grx3 as a reductant of insulin disulfides or as a hydrogen donor for ribonucleotide reductase. Thus, despite an identical active site disulfide motif and a similar secondary structure and tertiary fold, Grx3 and Grx1 display large functional differences in in vitro protein disulfide oxido-reduction reactions.
DOI: 10.1074/jbc.271.12.6736
PubMed: 8636094
Affiliations:
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Nordstrand</name></author><author><name sortKey="Berndt, K D" sort="Berndt, K D" uniqKey="Berndt K" first="K D" last="Berndt">K D Berndt</name></author><author><name sortKey="Nikkola, M" sort="Nikkola, M" uniqKey="Nikkola M" first="M" last="Nikkola">M. Nikkola</name></author><author><name sortKey="Bergman, T" sort="Bergman, T" uniqKey="Bergman T" first="T" last="Bergman">T. Bergman</name></author><author><name sortKey="Ponstingl, H" sort="Ponstingl, H" uniqKey="Ponstingl H" first="H" last="Ponstingl">H. Ponstingl</name></author><author><name sortKey="Jornvall, H" sort="Jornvall, H" uniqKey="Jornvall H" first="H" last="Jörnvall">H. Jörnvall</name></author><author><name sortKey="Otting, G" sort="Otting, G" uniqKey="Otting G" first="G" last="Otting">G. Otting</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1996">1996</date><idno type="RBID">pubmed:8636094</idno><idno type="pmid">8636094</idno><idno type="doi">10.1074/jbc.271.12.6736</idno><idno type="wicri:Area/Main/Corpus">001200</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001200</idno><idno type="wicri:Area/Main/Curation">001200</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001200</idno><idno type="wicri:Area/Main/Exploration">001200</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysis.</title><author><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. Aslund</name><affiliation wicri:level="1"><nlm:affiliation>Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77 Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77 Stockholm</wicri:regionArea><wicri:noRegion>S-171 77 Stockholm</wicri:noRegion></affiliation></author><author><name sortKey="Nordstrand, K" sort="Nordstrand, K" uniqKey="Nordstrand K" first="K" last="Nordstrand">K. Nordstrand</name></author><author><name sortKey="Berndt, K D" sort="Berndt, K D" uniqKey="Berndt K" first="K D" last="Berndt">K D Berndt</name></author><author><name sortKey="Nikkola, M" sort="Nikkola, M" uniqKey="Nikkola M" first="M" last="Nikkola">M. Nikkola</name></author><author><name sortKey="Bergman, T" sort="Bergman, T" uniqKey="Bergman T" first="T" last="Bergman">T. Bergman</name></author><author><name sortKey="Ponstingl, H" sort="Ponstingl, H" uniqKey="Ponstingl H" first="H" last="Ponstingl">H. Ponstingl</name></author><author><name sortKey="Jornvall, H" sort="Jornvall, H" uniqKey="Jornvall H" first="H" last="Jörnvall">H. Jörnvall</name></author><author><name sortKey="Otting, G" sort="Otting, G" uniqKey="Otting G" first="G" last="Otting">G. Otting</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1996" type="published">1996</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Disulfides (metabolism)</term><term>Escherichia coli (chemistry)</term><term>Glutaredoxins (MeSH)</term><term>Magnetic Resonance Spectroscopy (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Nitrogen Isotopes (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Proteins (chemistry)</term><term>Proteins (metabolism)</term><term>Protons (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines (MeSH)</term><term>Disulfures (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (composition chimique)</term><term>Glutarédoxines (MeSH)</term><term>Isotopes de l'azote (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Protons (MeSH)</term><term>Protéines (composition chimique)</term><term>Protéines (métabolisme)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Spectroscopie par résonance magnétique (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Disulfides</term><term>Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Escherichia coli</term><term>Protéines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Disulfures</term><term>Protéines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Glutaredoxins</term><term>Magnetic Resonance Spectroscopy</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Nitrogen Isotopes</term><term>Oxidoreductases</term><term>Protein Conformation</term><term>Protons</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Isotopes de l'azote</term><term>Modèles moléculaires</term><term>Oxidoreductases</term><term>Protons</term><term>Similitude de séquences d'acides aminés</term><term>Spectroscopie par résonance magnétique</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The primary and secondary structure of glutaredoxin-3 (Grx3), a glutathione-disulfide oxidoreductase from Escherichia coli, has been determined. The amino acid sequence of Grx3 consists of 82 residues and contains a redox-active motif, Cys-Pro-Tyr-Cys, typical of the glutaredoxin family. Sequence comparison reveals a homology (33% identity) to that of glutaredoxin-1 (Grx1) from E. coli as well as to other members of the thioredoxin superfamily. In addition to the active site cysteine residues, Grx3 contains one additional cysteine (Cys65) corresponding to one of the two non-active site (or structural) cysteine residues present in mammalian glutaredoxins. The sequence-specific 1H and 15N nuclear magnetic resonance assignments of reduced Grx3 have been obtained. From a combined analysis of chemical shifts, 3JHNalpha coupling constants, sequential and medium range NOEs, and amide proton exchange rates, the secondary structure of reduced Grx3 was determined and found to be very similar to that inferred from amino acid sequence comparison to homologous proteins. The consequences of the proposed structural similarity to Grx1 are that Grx3, while possessing a largely intact GSH binding cleft, would have a very different spatial distribution of charged residues, most notably surrounding the active site cysteine residues and occurring in the proposed hydrophobic protein-protein interaction area. These differences may contribute to the observed very low Kcat of Grx3 as a reductant of insulin disulfides or as a hydrogen donor for ribonucleotide reductase. Thus, despite an identical active site disulfide motif and a similar secondary structure and tertiary fold, Grx3 and Grx1 display large functional differences in in vitro protein disulfide oxido-reduction reactions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8636094</PMID><DateCompleted><Year>1996</Year><Month>07</Month><Day>09</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>271</Volume><Issue>12</Issue><PubDate><Year>1996</Year><Month>Mar</Month><Day>22</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysis.</ArticleTitle><Pagination><MedlinePgn>6736-45</MedlinePgn></Pagination><Abstract><AbstractText>The primary and secondary structure of glutaredoxin-3 (Grx3), a glutathione-disulfide oxidoreductase from Escherichia coli, has been determined. The amino acid sequence of Grx3 consists of 82 residues and contains a redox-active motif, Cys-Pro-Tyr-Cys, typical of the glutaredoxin family. Sequence comparison reveals a homology (33% identity) to that of glutaredoxin-1 (Grx1) from E. coli as well as to other members of the thioredoxin superfamily. In addition to the active site cysteine residues, Grx3 contains one additional cysteine (Cys65) corresponding to one of the two non-active site (or structural) cysteine residues present in mammalian glutaredoxins. The sequence-specific 1H and 15N nuclear magnetic resonance assignments of reduced Grx3 have been obtained. From a combined analysis of chemical shifts, 3JHNalpha coupling constants, sequential and medium range NOEs, and amide proton exchange rates, the secondary structure of reduced Grx3 was determined and found to be very similar to that inferred from amino acid sequence comparison to homologous proteins. The consequences of the proposed structural similarity to Grx1 are that Grx3, while possessing a largely intact GSH binding cleft, would have a very different spatial distribution of charged residues, most notably surrounding the active site cysteine residues and occurring in the proposed hydrophobic protein-protein interaction area. These differences may contribute to the observed very low Kcat of Grx3 as a reductant of insulin disulfides or as a hydrogen donor for ribonucleotide reductase. Thus, despite an identical active site disulfide motif and a similar secondary structure and tertiary fold, Grx3 and Grx1 display large functional differences in in vitro protein disulfide oxido-reduction reactions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Aslund</LastName><ForeName>F</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77 Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nordstrand</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Berndt</LastName><ForeName>K D</ForeName><Initials>KD</Initials></Author><Author ValidYN="Y"><LastName>Nikkola</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Bergman</LastName><ForeName>T</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Ponstingl</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Jörnvall</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Otting</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>A</ForeName><Initials>A</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>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009587">Nitrogen Isotopes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011522">Protons</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</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="D009587" MajorTopicYN="N">Nitrogen Isotopes</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="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011522" MajorTopicYN="N">Protons</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1996</Year><Month>3</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1996</Year><Month>3</Month><Day>22</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1996</Year><Month>3</Month><Day>22</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8636094</ArticleId><ArticleId IdType="doi">10.1074/jbc.271.12.6736</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country></list><tree><noCountry><name sortKey="Bergman, T" sort="Bergman, T" uniqKey="Bergman T" first="T" last="Bergman">T. Bergman</name><name sortKey="Berndt, K D" sort="Berndt, K D" uniqKey="Berndt K" first="K D" last="Berndt">K D Berndt</name><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name><name sortKey="Jornvall, H" sort="Jornvall, H" uniqKey="Jornvall H" first="H" last="Jörnvall">H. Jörnvall</name><name sortKey="Nikkola, M" sort="Nikkola, M" uniqKey="Nikkola M" first="M" last="Nikkola">M. Nikkola</name><name sortKey="Nordstrand, K" sort="Nordstrand, K" uniqKey="Nordstrand K" first="K" last="Nordstrand">K. Nordstrand</name><name sortKey="Otting, G" sort="Otting, G" uniqKey="Otting G" first="G" last="Otting">G. Otting</name><name sortKey="Ponstingl, H" sort="Ponstingl, H" uniqKey="Ponstingl H" first="H" last="Ponstingl">H. Ponstingl</name></noCountry><country name="Suède"><noRegion><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. 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