Structural and functional characterization of a thioredoxin-like protein (Mt0807) from Methanobacterium thermoautotrophicum.
Identifieur interne : 000F08 ( Main/Exploration ); précédent : 000F07; suivant : 000F09Structural and functional characterization of a thioredoxin-like protein (Mt0807) from Methanobacterium thermoautotrophicum.
Auteurs : Godwin Y. Amegbey [Canada] ; Hassan Monzavi ; Bahram Habibi-Nazhad ; Sudeepa Bhattacharyya ; David S. WishartSource :
- Biochemistry [ 0006-2960 ] ; 2003.
Descripteurs français
- KwdFr :
- Archéobactéries (composition chimique), Conformation des protéines (MeSH), Données de séquences moléculaires (MeSH), Glutarédoxines (MeSH), Methanobacterium (composition chimique), Modèles moléculaires (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Pliage des protéines (MeSH), Protéines (composition chimique), Protéines bactériennes (composition chimique), Similitude de séquences d'acides aminés (MeSH), Sites de fixation (MeSH), Spectroscopie par résonance magnétique (MeSH), Séquence d'acides aminés (MeSH), Thermodynamique (MeSH), Thiorédoxines (composition chimique).
- MESH :
- composition chimique : Archéobactéries, Methanobacterium, Protéines, Protéines bactériennes, Thiorédoxines.
- Conformation des protéines, Données de séquences moléculaires, Glutarédoxines, Modèles moléculaires, Oxidoreductases, Oxydoréduction, Pliage des protéines, Similitude de séquences d'acides aminés, Sites de fixation, Spectroscopie par résonance magnétique, Séquence d'acides aminés, Thermodynamique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Archaea (chemistry), Bacterial Proteins (chemistry), Binding Sites (MeSH), Glutaredoxins (MeSH), Magnetic Resonance Spectroscopy (MeSH), Methanobacterium (chemistry), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Protein Conformation (MeSH), Protein Folding (MeSH), Proteins (chemistry), Sequence Homology, Amino Acid (MeSH), Thermodynamics (MeSH), Thioredoxins (chemistry).
- MESH :
- chemical , chemistry : Bacterial Proteins, Proteins, Thioredoxins.
- chemistry : Archaea, Methanobacterium.
- Amino Acid Sequence, Binding Sites, Glutaredoxins, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Oxidoreductases, Protein Conformation, Protein Folding, Sequence Homology, Amino Acid, Thermodynamics.
Abstract
Mt0807 is an 85-residue thiol-redox protein from the anaerobic archaebacterium Methanobacterium thermoautotrophicum. Its small size, its participation in certain redox reactions, and the presence of a "classic" glutareodoxin active-site sequence have led to the suggestion that it might be a glutaredoxin. However, studies by previous workers indicated that it exhibited neither glutaredoxin-like nor thioredoxin-like properties. To clarify the true role of this protein and its structure/functional relationship with a paralogous thioredoxin (Mt0895, 28% sequence identity) and a recently characterized orthologous protein (Mj0307, 51% sequence identity), we undertook a series of biochemical and biophysical studies. Comparative enzymatic assays and thiol titration experiments were combined with NMR structural studies and detailed 3D structure comparisons. Structurally, our results show that Mt0807 has a glutaredoxin-like fold (central four-stranded beta-sheet core surrounded by two helices on one side and a third on the other). However, more detailed comparisons with other members of the thioredoxin superfamily indicate that Mt0807 actually has several key structural and active-site characteristics more common to a thioredoxin. Furthermore, biochemical tests show that Mt0807 actually behaves as true thioredoxin. Comparisons between Mt0807 and its paralogue, Mt0895, indicate these two archaebacterial thioredoxins share very similar folds, but exhibit very different activities and likely serve somewhat different roles. On the basis of its greater relative abundance and significantly stronger redox activity, we believe that Mt0807 is the primary thioredoxin for M. thermoautotrophicum, while Mt0895 plays a minor or supportive role. We also suggest that these two molecules (Mt0807 and Mt0895) may represent a group of ancient proteins that were ancestral to both thioredoxins and glutaredoxins.
DOI: 10.1021/bi030021g
PubMed: 12834352
Affiliations:
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Its small size, its participation in certain redox reactions, and the presence of a "classic" glutareodoxin active-site sequence have led to the suggestion that it might be a glutaredoxin. However, studies by previous workers indicated that it exhibited neither glutaredoxin-like nor thioredoxin-like properties. To clarify the true role of this protein and its structure/functional relationship with a paralogous thioredoxin (Mt0895, 28% sequence identity) and a recently characterized orthologous protein (Mj0307, 51% sequence identity), we undertook a series of biochemical and biophysical studies. Comparative enzymatic assays and thiol titration experiments were combined with NMR structural studies and detailed 3D structure comparisons. Structurally, our results show that Mt0807 has a glutaredoxin-like fold (central four-stranded beta-sheet core surrounded by two helices on one side and a third on the other). However, more detailed comparisons with other members of the thioredoxin superfamily indicate that Mt0807 actually has several key structural and active-site characteristics more common to a thioredoxin. Furthermore, biochemical tests show that Mt0807 actually behaves as true thioredoxin. Comparisons between Mt0807 and its paralogue, Mt0895, indicate these two archaebacterial thioredoxins share very similar folds, but exhibit very different activities and likely serve somewhat different roles. On the basis of its greater relative abundance and significantly stronger redox activity, we believe that Mt0807 is the primary thioredoxin for M. thermoautotrophicum, while Mt0895 plays a minor or supportive role. We also suggest that these two molecules (Mt0807 and Mt0895) may represent a group of ancient proteins that were ancestral to both thioredoxins and glutaredoxins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12834352</PMID><DateCompleted><Year>2003</Year><Month>08</Month><Day>22</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>42</Volume><Issue>26</Issue><PubDate><Year>2003</Year><Month>Jul</Month><Day>08</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Structural and functional characterization of a thioredoxin-like protein (Mt0807) from Methanobacterium thermoautotrophicum.</ArticleTitle><Pagination><MedlinePgn>8001-10</MedlinePgn></Pagination><Abstract><AbstractText>Mt0807 is an 85-residue thiol-redox protein from the anaerobic archaebacterium Methanobacterium thermoautotrophicum. Its small size, its participation in certain redox reactions, and the presence of a "classic" glutareodoxin active-site sequence have led to the suggestion that it might be a glutaredoxin. However, studies by previous workers indicated that it exhibited neither glutaredoxin-like nor thioredoxin-like properties. To clarify the true role of this protein and its structure/functional relationship with a paralogous thioredoxin (Mt0895, 28% sequence identity) and a recently characterized orthologous protein (Mj0307, 51% sequence identity), we undertook a series of biochemical and biophysical studies. Comparative enzymatic assays and thiol titration experiments were combined with NMR structural studies and detailed 3D structure comparisons. Structurally, our results show that Mt0807 has a glutaredoxin-like fold (central four-stranded beta-sheet core surrounded by two helices on one side and a third on the other). However, more detailed comparisons with other members of the thioredoxin superfamily indicate that Mt0807 actually has several key structural and active-site characteristics more common to a thioredoxin. Furthermore, biochemical tests show that Mt0807 actually behaves as true thioredoxin. Comparisons between Mt0807 and its paralogue, Mt0895, indicate these two archaebacterial thioredoxins share very similar folds, but exhibit very different activities and likely serve somewhat different roles. On the basis of its greater relative abundance and significantly stronger redox activity, we believe that Mt0807 is the primary thioredoxin for M. thermoautotrophicum, while Mt0895 plays a minor or supportive role. We also suggest that these two molecules (Mt0807 and Mt0895) may represent a group of ancient proteins that were ancestral to both thioredoxins and glutaredoxins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Amegbey</LastName><ForeName>Godwin Y</ForeName><Initials>GY</Initials><AffiliationInfo><Affiliation>Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, Edmonton, Canada T6G 2N8.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Monzavi</LastName><ForeName>Hassan</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Habibi-Nazhad</LastName><ForeName>Bahram</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Bhattacharyya</LastName><ForeName>Sudeepa</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Wishart</LastName><ForeName>David S</ForeName><Initials>DS</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><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>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance 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MajorTopicYN="N">Methanobacterium</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></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="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="Y">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2003</Year><Month>7</Month><Day>2</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>8</Month><Day>23</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2003</Year><Month>7</Month><Day>2</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12834352</ArticleId><ArticleId IdType="doi">10.1021/bi030021g</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country><region><li>Alberta</li></region><settlement><li>Edmonton</li></settlement></list><tree><noCountry><name sortKey="Bhattacharyya, Sudeepa" sort="Bhattacharyya, Sudeepa" uniqKey="Bhattacharyya S" first="Sudeepa" last="Bhattacharyya">Sudeepa Bhattacharyya</name><name sortKey="Habibi Nazhad, Bahram" sort="Habibi Nazhad, Bahram" uniqKey="Habibi Nazhad B" first="Bahram" last="Habibi-Nazhad">Bahram Habibi-Nazhad</name><name sortKey="Monzavi, Hassan" sort="Monzavi, Hassan" uniqKey="Monzavi H" first="Hassan" last="Monzavi">Hassan Monzavi</name><name sortKey="Wishart, David S" sort="Wishart, David S" uniqKey="Wishart D" first="David S" last="Wishart">David S. Wishart</name></noCountry><country name="Canada"><region name="Alberta"><name sortKey="Amegbey, Godwin Y" sort="Amegbey, Godwin Y" uniqKey="Amegbey G" first="Godwin Y" last="Amegbey">Godwin Y. Amegbey</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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