Structural and Biochemical Characterizations of Methanoredoxin from Methanosarcina acetivorans, a Glutaredoxin-Like Enzyme with Coenzyme M-Dependent Protein Disulfide Reductase Activity.
Identifieur interne : 000415 ( Main/Exploration ); précédent : 000414; suivant : 000416Structural and Biochemical Characterizations of Methanoredoxin from Methanosarcina acetivorans, a Glutaredoxin-Like Enzyme with Coenzyme M-Dependent Protein Disulfide Reductase Activity.
Auteurs : Deepa Yenugudhati [États-Unis] ; Divya Prakash [États-Unis] ; Adepu K. Kumar [États-Unis] ; R Siva Sai Kumar [États-Unis] ; Neela H. Yennawar [États-Unis] ; Hemant P. Yennawar [États-Unis] ; James G. Ferry [États-Unis]Source :
- Biochemistry [ 1520-4995 ] ; 2016.
Descripteurs français
- KwdFr :
- Glutarédoxines (composition chimique), Glutarédoxines (métabolisme), Mesna (métabolisme), Methanosarcina (métabolisme), Protein-disulfide reductase (glutathione) (composition chimique), Protein-disulfide reductase (glutathione) (métabolisme), Protéines d'archée (composition chimique), Protéines d'archée (métabolisme), Structure secondaire des protéines (MeSH).
- MESH :
- composition chimique : Glutarédoxines, Protein-disulfide reductase (glutathione), Protéines d'archée.
- métabolisme : Glutarédoxines, Mesna, Methanosarcina, Protein-disulfide reductase (glutathione), Protéines d'archée.
- Structure secondaire des protéines.
English descriptors
- KwdEn :
- Archaeal Proteins (chemistry), Archaeal Proteins (metabolism), Glutaredoxins (chemistry), Glutaredoxins (metabolism), Mesna (metabolism), Methanosarcina (metabolism), Protein Disulfide Reductase (Glutathione) (chemistry), Protein Disulfide Reductase (Glutathione) (metabolism), Protein Structure, Secondary (MeSH).
- MESH :
- chemical , chemistry : Archaeal Proteins, Glutaredoxins, Protein Disulfide Reductase (Glutathione).
- chemical , metabolism : Archaeal Proteins, Glutaredoxins, Mesna, Protein Disulfide Reductase (Glutathione).
- metabolism : Methanosarcina.
- Protein Structure, Secondary.
Abstract
Glutaredoxins (GRXs) are thiol-disulfide oxidoreductases abundant in prokaryotes, although little is understood of these enzymes from the domain Archaea. The numerous characterized GRXs from the domain Bacteria utilize a diversity of low-molecular-weight thiols in addition to glutathione as reductants. We report here the biochemical and structural properties of a GRX-like protein named methanoredoxin (MRX) from Methanosarcina acetivorans of the domain Archaea. MRX utilizes coenzyme M (CoMSH) as reductant for insulin disulfide reductase activity, which adds to the diversity of thiol protectants in prokaryotes. Cell-free extracts of M. acetivorans displayed CoMS-SCoM reductase activity that complements the CoMSH-dependent activity of MRX. The crystal structure exhibits a classic thioredoxin-glutaredoxin fold comprising three α-helices surrounding four antiparallel β-sheets. A pocket on the surface contains a CVWC motif, identifying the active site with architecture similar to GRXs. Although it is a monomer in solution, the crystal lattice has four monomers in a dimer of dimers arrangement. A cadmium ion is found within the active site of each monomer. Two such ions stabilize the N-terminal tails and dimer interfaces. Our modeling studies indicate that CoMSH and glutathione (GSH) bind to the active site of MRX similar to the binding of GSH in GRXs, although there are differences in the amino acid composition of the binding motifs. The results, combined with our bioinformatic analyses, show that MRX represents a class of GRX-like enzymes present in a diversity of methane-producing Archaea.
DOI: 10.1021/acs.biochem.5b00823
PubMed: 26684934
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Kumar</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802</wicri:regionArea><wicri:noRegion>Pennsylvania 16802</wicri:noRegion></affiliation></author><author><name sortKey="Kumar, R Siva Sai" sort="Kumar, R Siva Sai" uniqKey="Kumar R" first="R Siva Sai" last="Kumar">R Siva Sai Kumar</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802</wicri:regionArea><wicri:noRegion>Pennsylvania 16802</wicri:noRegion></affiliation></author><author><name sortKey="Yennawar, Neela H" sort="Yennawar, Neela H" uniqKey="Yennawar N" first="Neela H" last="Yennawar">Neela H. Yennawar</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802</wicri:regionArea><wicri:noRegion>Pennsylvania 16802</wicri:noRegion></affiliation></author><author><name sortKey="Yennawar, Hemant P" sort="Yennawar, Hemant P" uniqKey="Yennawar H" first="Hemant P" last="Yennawar">Hemant P. Yennawar</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802</wicri:regionArea><wicri:noRegion>Pennsylvania 16802</wicri:noRegion></affiliation></author><author><name sortKey="Ferry, James G" sort="Ferry, James G" uniqKey="Ferry J" first="James G" last="Ferry">James G. Ferry</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802</wicri:regionArea><wicri:noRegion>Pennsylvania 16802</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochemistry</title><idno type="eISSN">1520-4995</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Archaeal Proteins (chemistry)</term><term>Archaeal Proteins (metabolism)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (metabolism)</term><term>Mesna (metabolism)</term><term>Methanosarcina (metabolism)</term><term>Protein Disulfide Reductase (Glutathione) (chemistry)</term><term>Protein Disulfide Reductase (Glutathione) (metabolism)</term><term>Protein Structure, Secondary (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (métabolisme)</term><term>Mesna (métabolisme)</term><term>Methanosarcina (métabolisme)</term><term>Protein-disulfide reductase (glutathione) (composition chimique)</term><term>Protein-disulfide reductase (glutathione) (métabolisme)</term><term>Protéines d'archée (composition chimique)</term><term>Protéines d'archée (métabolisme)</term><term>Structure secondaire des protéines (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Archaeal Proteins</term><term>Glutaredoxins</term><term>Protein Disulfide Reductase (Glutathione)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Archaeal Proteins</term><term>Glutaredoxins</term><term>Mesna</term><term>Protein Disulfide Reductase (Glutathione)</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term><term>Protein-disulfide reductase (glutathione)</term><term>Protéines d'archée</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Methanosarcina</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term><term>Mesna</term><term>Methanosarcina</term><term>Protein-disulfide reductase (glutathione)</term><term>Protéines d'archée</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Protein Structure, Secondary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Structure secondaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins (GRXs) are thiol-disulfide oxidoreductases abundant in prokaryotes, although little is understood of these enzymes from the domain Archaea. The numerous characterized GRXs from the domain Bacteria utilize a diversity of low-molecular-weight thiols in addition to glutathione as reductants. We report here the biochemical and structural properties of a GRX-like protein named methanoredoxin (MRX) from Methanosarcina acetivorans of the domain Archaea. MRX utilizes coenzyme M (CoMSH) as reductant for insulin disulfide reductase activity, which adds to the diversity of thiol protectants in prokaryotes. Cell-free extracts of M. acetivorans displayed CoMS-SCoM reductase activity that complements the CoMSH-dependent activity of MRX. The crystal structure exhibits a classic thioredoxin-glutaredoxin fold comprising three α-helices surrounding four antiparallel β-sheets. A pocket on the surface contains a CVWC motif, identifying the active site with architecture similar to GRXs. Although it is a monomer in solution, the crystal lattice has four monomers in a dimer of dimers arrangement. A cadmium ion is found within the active site of each monomer. Two such ions stabilize the N-terminal tails and dimer interfaces. Our modeling studies indicate that CoMSH and glutathione (GSH) bind to the active site of MRX similar to the binding of GSH in GRXs, although there are differences in the amino acid composition of the binding motifs. The results, combined with our bioinformatic analyses, show that MRX represents a class of GRX-like enzymes present in a diversity of methane-producing Archaea. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26684934</PMID><DateCompleted><Year>2016</Year><Month>05</Month><Day>23</Day></DateCompleted><DateRevised><Year>2016</Year><Month>01</Month><Day>19</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-4995</ISSN><JournalIssue CitedMedium="Internet"><Volume>55</Volume><Issue>2</Issue><PubDate><Year>2016</Year><Month>Jan</Month><Day>19</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Structural and Biochemical Characterizations of Methanoredoxin from Methanosarcina acetivorans, a Glutaredoxin-Like Enzyme with Coenzyme M-Dependent Protein Disulfide Reductase Activity.</ArticleTitle><Pagination><MedlinePgn>313-21</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/acs.biochem.5b00823</ELocationID><Abstract><AbstractText>Glutaredoxins (GRXs) are thiol-disulfide oxidoreductases abundant in prokaryotes, although little is understood of these enzymes from the domain Archaea. The numerous characterized GRXs from the domain Bacteria utilize a diversity of low-molecular-weight thiols in addition to glutathione as reductants. We report here the biochemical and structural properties of a GRX-like protein named methanoredoxin (MRX) from Methanosarcina acetivorans of the domain Archaea. MRX utilizes coenzyme M (CoMSH) as reductant for insulin disulfide reductase activity, which adds to the diversity of thiol protectants in prokaryotes. Cell-free extracts of M. acetivorans displayed CoMS-SCoM reductase activity that complements the CoMSH-dependent activity of MRX. The crystal structure exhibits a classic thioredoxin-glutaredoxin fold comprising three α-helices surrounding four antiparallel β-sheets. A pocket on the surface contains a CVWC motif, identifying the active site with architecture similar to GRXs. Although it is a monomer in solution, the crystal lattice has four monomers in a dimer of dimers arrangement. A cadmium ion is found within the active site of each monomer. Two such ions stabilize the N-terminal tails and dimer interfaces. Our modeling studies indicate that CoMSH and glutathione (GSH) bind to the active site of MRX similar to the binding of GSH in GRXs, although there are differences in the amino acid composition of the binding motifs. The results, combined with our bioinformatic analyses, show that MRX represents a class of GRX-like enzymes present in a diversity of methane-producing Archaea. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yenugudhati</LastName><ForeName>Deepa</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Prakash</LastName><ForeName>Divya</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kumar</LastName><ForeName>Adepu K</ForeName><Initials>AK</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kumar</LastName><ForeName>R Siva Sai</ForeName><Initials>RS</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yennawar</LastName><ForeName>Neela H</ForeName><Initials>NH</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yennawar</LastName><ForeName>Hemant P</ForeName><Initials>HP</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ferry</LastName><ForeName>James G</ForeName><Initials>JG</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, ‡Huck Institutes of Life Sciences, The Pennsylvania State University , University Park, Pennsylvania 16802, United States.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>1S10RR023439-01</GrantID><Acronym>RR</Acronym><Agency>NCRR NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>12</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019843">Archaeal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical><Chemical><RegistryNumber>NR7O1405Q9</RegistryNumber><NameOfSubstance UI="D015080">Mesna</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019843" MajorTopicYN="N">Archaeal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015080" MajorTopicYN="N">Mesna</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017020" MajorTopicYN="N">Methanosarcina</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="N">Protein Disulfide Reductase (Glutathione)</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>12</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>12</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>5</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26684934</ArticleId><ArticleId IdType="doi">10.1021/acs.biochem.5b00823</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Yenugudhati, Deepa" sort="Yenugudhati, Deepa" uniqKey="Yenugudhati D" first="Deepa" last="Yenugudhati">Deepa Yenugudhati</name></noRegion><name sortKey="Ferry, James G" sort="Ferry, James G" uniqKey="Ferry J" first="James G" last="Ferry">James G. Ferry</name><name sortKey="Kumar, Adepu K" sort="Kumar, Adepu K" uniqKey="Kumar A" first="Adepu K" last="Kumar">Adepu K. Kumar</name><name sortKey="Kumar, R Siva Sai" sort="Kumar, R Siva Sai" uniqKey="Kumar R" first="R Siva Sai" last="Kumar">R Siva Sai Kumar</name><name sortKey="Prakash, Divya" sort="Prakash, Divya" uniqKey="Prakash D" first="Divya" last="Prakash">Divya Prakash</name><name sortKey="Yennawar, Hemant P" sort="Yennawar, Hemant P" uniqKey="Yennawar H" first="Hemant P" last="Yennawar">Hemant P. Yennawar</name><name sortKey="Yennawar, Neela H" sort="Yennawar, Neela H" uniqKey="Yennawar N" first="Neela H" last="Yennawar">Neela H. Yennawar</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:26684934" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |