GlutaredoxinV1, Main, Exploration, bibRecord, 000F81

Identification of a novel archaebacterial thioredoxin: determination of function through structure.

Identifieur interne : 000F81 ( Main/Exploration ); précédent : 000F80; suivant : 000F82

Identification of a novel archaebacterial thioredoxin: determination of function through structure.

Auteurs : Sudeepa Bhattacharyya [Canada] ; Bahram Habibi-Nazhad ; Godwin Amegbey ; Carolyn M. Slupsky ; Adelinda Yee ; Cheryl Arrowsmith ; David S. Wishart

Source :

Biochemistry [ 0006-2960 ] ; 2002.

RBID : pubmed:11939770

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Binding Sites (MeSH), Conserved Sequence (MeSH), DNA-Directed DNA Polymerase (metabolism), Magnetic Resonance Spectroscopy (MeSH), Methanobacterium (metabolism), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Protein Conformation (MeSH), Sequence Alignment (MeSH), Solutions (MeSH), Thermodynamics (MeSH), Thioredoxins (chemistry), Thioredoxins (metabolism).
MESH :
- chemical , chemistry : Thioredoxins.
- chemical , metabolism : DNA-Directed DNA Polymerase, Thioredoxins.
- metabolism : Methanobacterium.
- Amino Acid Sequence, Binding Sites, Conserved Sequence, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Protein Conformation, Sequence Alignment, Solutions, Thermodynamics.

Abstract

As part of a high-throughput, structural proteomic project we have used NMR spectroscopy to determine the solution structure and ascertain the function of a previously unknown, conserved protein (MtH895) from the thermophilic archeon Methanobacterium thermoautotrophicum. Our findings indicate that MtH895 contains a central four-stranded beta-sheet core surrounded by two helices on one side and a third on the other. It has an overall fold superficially similar to that of a glutaredoxin. However, detailed analysis of its three-dimensional structure along with molecular docking simulations of its interaction with T7 DNA polymerase (a thioredoxin-specific substrate) and comparisons with other known members of the thioredoxin/glutaredoxin family of proteins strongly suggest that MtH895 is more akin to a thioredoxin. Furthermore, measurement of the pK(a) values of its active site thiols along with direct measurements of the thioredoxin/glutaredoxin activity has confirmed that MtH895 is, indeed, a thioredoxin and exhibits no glutaredoxin activity. We have also identified a group of previously unknown proteins from several other archaebacteria that have significant (34-44%) sequence identity with MtH895. These proteins have unusual active site -CXXC- motifs not found in any known thioredoxin or glutaredoxin. On the basis of the results presented here, we predict that these small proteins are all members of a new class of truncated thioredoxins.

DOI: 10.1021/bi0115176
PubMed: 11939770

Affiliations:

Canada

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

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Le document en format XML

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<author><name sortKey="Bhattacharyya, Sudeepa" sort="Bhattacharyya, Sudeepa" uniqKey="Bhattacharyya S" first="Sudeepa" last="Bhattacharyya">Sudeepa Bhattacharyya</name>
<affiliation wicri:level="1"><nlm:affiliation>Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, Edmonton, Alberta, Canada.</nlm:affiliation>
<country xml:lang="fr">Canada</country>
<wicri:regionArea>Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, Edmonton, Alberta</wicri:regionArea>
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<author><name sortKey="Habibi Nazhad, Bahram" sort="Habibi Nazhad, Bahram" uniqKey="Habibi Nazhad B" first="Bahram" last="Habibi-Nazhad">Bahram Habibi-Nazhad</name>
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<author><name sortKey="Slupsky, Carolyn M" sort="Slupsky, Carolyn M" uniqKey="Slupsky C" first="Carolyn M" last="Slupsky">Carolyn M. Slupsky</name>
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<term>DNA-Directed DNA Polymerase (metabolism)</term>
<term>Magnetic Resonance Spectroscopy (MeSH)</term>
<term>Methanobacterium (metabolism)</term>
<term>Models, Molecular (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Protein Conformation (MeSH)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Solutions (MeSH)</term>
<term>Thermodynamics (MeSH)</term>
<term>Thioredoxins (chemistry)</term>
<term>Thioredoxins (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term>
<term>Conformation des protéines (MeSH)</term>
<term>DNA-directed DNA polymerase (métabolisme)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Methanobacterium (métabolisme)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Sites de fixation (MeSH)</term>
<term>Solutions (MeSH)</term>
<term>Spectroscopie par résonance magnétique (MeSH)</term>
<term>Séquence conservée (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Thermodynamique (MeSH)</term>
<term>Thiorédoxines (composition chimique)</term>
<term>Thiorédoxines (métabolisme)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Thioredoxins</term>
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<term>Protein Conformation</term>
<term>Sequence Alignment</term>
<term>Solutions</term>
<term>Thermodynamics</term>
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<term>Conformation des protéines</term>
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<term>Modèles moléculaires</term>
<term>Sites de fixation</term>
<term>Solutions</term>
<term>Spectroscopie par résonance magnétique</term>
<term>Séquence conservée</term>
<term>Séquence d'acides aminés</term>
<term>Thermodynamique</term>
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<front><div type="abstract" xml:lang="en">As part of a high-throughput, structural proteomic project we have used NMR spectroscopy to determine the solution structure and ascertain the function of a previously unknown, conserved protein (MtH895) from the thermophilic archeon Methanobacterium thermoautotrophicum. Our findings indicate that MtH895 contains a central four-stranded beta-sheet core surrounded by two helices on one side and a third on the other. It has an overall fold superficially similar to that of a glutaredoxin. However, detailed analysis of its three-dimensional structure along with molecular docking simulations of its interaction with T7 DNA polymerase (a thioredoxin-specific substrate) and comparisons with other known members of the thioredoxin/glutaredoxin family of proteins strongly suggest that MtH895 is more akin to a thioredoxin. Furthermore, measurement of the pK(a) values of its active site thiols along with direct measurements of the thioredoxin/glutaredoxin activity has confirmed that MtH895 is, indeed, a thioredoxin and exhibits no glutaredoxin activity. We have also identified a group of previously unknown proteins from several other archaebacteria that have significant (34-44%) sequence identity with MtH895. These proteins have unusual active site -CXXC- motifs not found in any known thioredoxin or glutaredoxin. On the basis of the results presented here, we predict that these small proteins are all members of a new class of truncated thioredoxins.</div>
</front>
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<Abstract><AbstractText>As part of a high-throughput, structural proteomic project we have used NMR spectroscopy to determine the solution structure and ascertain the function of a previously unknown, conserved protein (MtH895) from the thermophilic archeon Methanobacterium thermoautotrophicum. Our findings indicate that MtH895 contains a central four-stranded beta-sheet core surrounded by two helices on one side and a third on the other. It has an overall fold superficially similar to that of a glutaredoxin. However, detailed analysis of its three-dimensional structure along with molecular docking simulations of its interaction with T7 DNA polymerase (a thioredoxin-specific substrate) and comparisons with other known members of the thioredoxin/glutaredoxin family of proteins strongly suggest that MtH895 is more akin to a thioredoxin. Furthermore, measurement of the pK(a) values of its active site thiols along with direct measurements of the thioredoxin/glutaredoxin activity has confirmed that MtH895 is, indeed, a thioredoxin and exhibits no glutaredoxin activity. We have also identified a group of previously unknown proteins from several other archaebacteria that have significant (34-44%) sequence identity with MtH895. These proteins have unusual active site -CXXC- motifs not found in any known thioredoxin or glutaredoxin. On the basis of the results presented here, we predict that these small proteins are all members of a new class of truncated thioredoxins.</AbstractText>
</Abstract>
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<name sortKey="Habibi Nazhad, Bahram" sort="Habibi Nazhad, Bahram" uniqKey="Habibi Nazhad B" first="Bahram" last="Habibi-Nazhad">Bahram Habibi-Nazhad</name>
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Serveur d'exploration sur la glutarédoxine

Identification of a novel archaebacterial thioredoxin: determination of function through structure.

Identification of a novel archaebacterial thioredoxin: determination of function through structure.

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