Structural insights into the binding of buckwheat glutaredoxin with GSH and regulation of its catalytic activity.
Identifieur interne : 000309 ( Main/Exploration ); précédent : 000308; suivant : 000310Structural insights into the binding of buckwheat glutaredoxin with GSH and regulation of its catalytic activity.
Auteurs : Xinyu Zhang [République populaire de Chine] ; Wenming Wang [République populaire de Chine] ; Chen Li [République populaire de Chine] ; Yi Zhao [République populaire de Chine] ; Hong Yuan [République populaire de Chine] ; Xianshi Tan [République populaire de Chine] ; Lijie Wu [République populaire de Chine] ; Zhuanhua Wang [République populaire de Chine] ; Hongfei Wang [République populaire de Chine]Source :
- Journal of inorganic biochemistry [ 1873-3344 ] ; 2017.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Glutarédoxines, Glutathion, Protéines végétales.
- métabolisme : Fagopyrum, Glutarédoxines, Glutathion, Protéines végétales.
- Diffraction des rayons X, Liaison aux protéines.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Glutaredoxins, Glutathione, Plant Proteins.
- metabolism : Fagopyrum, Glutaredoxins, Glutathione, Plant Proteins.
- Protein Binding, X-Ray Diffraction.
Abstract
Glutaredoxins (Grxs) are ubiquitous thioltransferases and members of the thioredoxin (Trx) fold superfamily. They have multiple functions in cells including oxidative stress responses and cell signaling. A novel glutaredoxin from buckwheat (rbGrx) with higher catalytic activity was identified, cloned, and purified. The structures of glutathionylated rbGrx and an rbGrx mutant, in which cysteine 39 was mutated to alanine, were solved by x-ray diffraction at a resolution of 2.05Å and 2.29Å, respectively. In rbGrx, GSH (glutathione) is bound at the conserved GSH-binding site, and its structure shows that it has the potential to function as a scaffold protein for the assembly and delivery of GSH. The crystal structure shows that GSH does not bind to the C39A rbGrx mutant, and the C39A mutant had no catalytic activity, indicating that C39 is a key residue that is involved in both the binding of rbGrx to GSH and the regulation of its catalytic activity. The model showing the binding of GSH with rbGrx provides a basis for understanding its molecular function and its potential future applications in medicinal food science.
DOI: 10.1016/j.jinorgbio.2017.04.019
PubMed: 28478310
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Electronic address: zhwang@sxu.edu.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Life Science, Shanxi University, Shanxi, Taiyuan 030006</wicri:regionArea><wicri:noRegion>Taiyuan 030006</wicri:noRegion></affiliation></author><author><name sortKey="Wang, Hongfei" sort="Wang, Hongfei" uniqKey="Wang H" first="Hongfei" last="Wang">Hongfei Wang</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Molecular Science, Shanxi University, Shanxi, Taiyuan 030006, China. Electronic address: wanghf@sxu.edu.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Institute of Molecular Science, Shanxi University, Shanxi, Taiyuan 030006</wicri:regionArea><wicri:noRegion>Taiyuan 030006</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of inorganic biochemistry</title><idno type="eISSN">1873-3344</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Fagopyrum (metabolism)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (genetics)</term><term>Glutathione (metabolism)</term><term>Plant Proteins (genetics)</term><term>Plant Proteins (metabolism)</term><term>Protein Binding (MeSH)</term><term>X-Ray Diffraction (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Diffraction des rayons X (MeSH)</term><term>Fagopyrum (métabolisme)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (génétique)</term><term>Glutathion (métabolisme)</term><term>Liaison aux protéines (MeSH)</term><term>Protéines végétales (génétique)</term><term>Protéines végétales (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>Glutathione</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term><term>Glutathion</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Fagopyrum</term><term>Glutaredoxins</term><term>Glutathione</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fagopyrum</term><term>Glutarédoxines</term><term>Glutathion</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Protein Binding</term><term>X-Ray Diffraction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Diffraction des rayons X</term><term>Liaison aux protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins (Grxs) are ubiquitous thioltransferases and members of the thioredoxin (Trx) fold superfamily. They have multiple functions in cells including oxidative stress responses and cell signaling. A novel glutaredoxin from buckwheat (rbGrx) with higher catalytic activity was identified, cloned, and purified. The structures of glutathionylated rbGrx and an rbGrx mutant, in which cysteine 39 was mutated to alanine, were solved by x-ray diffraction at a resolution of 2.05Å and 2.29Å, respectively. In rbGrx, GSH (glutathione) is bound at the conserved GSH-binding site, and its structure shows that it has the potential to function as a scaffold protein for the assembly and delivery of GSH. The crystal structure shows that GSH does not bind to the C39A rbGrx mutant, and the C39A mutant had no catalytic activity, indicating that C39 is a key residue that is involved in both the binding of rbGrx to GSH and the regulation of its catalytic activity. The model showing the binding of GSH with rbGrx provides a basis for understanding its molecular function and its potential future applications in medicinal food science.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28478310</PMID><DateCompleted><Year>2017</Year><Month>12</Month><Day>27</Day></DateCompleted><DateRevised><Year>2018</Year><Month>03</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-3344</ISSN><JournalIssue CitedMedium="Internet"><Volume>173</Volume><PubDate><Year>2017</Year><Month>08</Month></PubDate></JournalIssue><Title>Journal of inorganic biochemistry</Title><ISOAbbreviation>J Inorg Biochem</ISOAbbreviation></Journal><ArticleTitle>Structural insights into the binding of buckwheat glutaredoxin with GSH and regulation of its catalytic activity.</ArticleTitle><Pagination><MedlinePgn>21-27</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0162-0134(16)30482-2</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jinorgbio.2017.04.019</ELocationID><Abstract><AbstractText>Glutaredoxins (Grxs) are ubiquitous thioltransferases and members of the thioredoxin (Trx) fold superfamily. They have multiple functions in cells including oxidative stress responses and cell signaling. A novel glutaredoxin from buckwheat (rbGrx) with higher catalytic activity was identified, cloned, and purified. The structures of glutathionylated rbGrx and an rbGrx mutant, in which cysteine 39 was mutated to alanine, were solved by x-ray diffraction at a resolution of 2.05Å and 2.29Å, respectively. In rbGrx, GSH (glutathione) is bound at the conserved GSH-binding site, and its structure shows that it has the potential to function as a scaffold protein for the assembly and delivery of GSH. The crystal structure shows that GSH does not bind to the C39A rbGrx mutant, and the C39A mutant had no catalytic activity, indicating that C39 is a key residue that is involved in both the binding of rbGrx to GSH and the regulation of its catalytic activity. The model showing the binding of GSH with rbGrx provides a basis for understanding its molecular function and its potential future applications in medicinal food science.</AbstractText><CopyrightInformation>Copyright © 2017 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Xinyu</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>College of Life Science, Shanxi University, Shanxi, Taiyuan 030006, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Wenming</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Institute of Molecular Science, Shanxi University, Shanxi, Taiyuan 030006, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Chen</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>College of Life Science, Shanxi University, Shanxi, Taiyuan 030006, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhao</LastName><ForeName>Yi</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Biology Institute of Shanxi, Shanxi, Taiyuan 030006, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yuan</LastName><ForeName>Hong</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Fudan University, Shanghai 200433, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tan</LastName><ForeName>Xianshi</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Fudan University, Shanghai 200433, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Lijie</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>National Center for Protein Science Shanghai, Shanghai Institutes of Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Zhuanhua</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>College of Life Science, Shanxi University, Shanxi, Taiyuan 030006, China. Electronic address: zhwang@sxu.edu.cn.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Hongfei</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Institute of Molecular Science, Shanxi University, Shanxi, Taiyuan 030006, China. Electronic address: wanghf@sxu.edu.cn.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>04</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Inorg Biochem</MedlineTA><NlmUniqueID>7905788</NlmUniqueID><ISSNLinking>0162-0134</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019612" MajorTopicYN="N">Fagopyrum</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014961" MajorTopicYN="N">X-Ray Diffraction</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Crystal structure</Keyword><Keyword MajorTopicYN="Y">Enzymatic activity</Keyword><Keyword MajorTopicYN="Y">Glutaredoxin</Keyword><Keyword MajorTopicYN="Y">Glutathione</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>12</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2017</Year><Month>04</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>04</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>5</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>12</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>5</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28478310</ArticleId><ArticleId IdType="pii">S0162-0134(16)30482-2</ArticleId><ArticleId IdType="doi">10.1016/j.jinorgbio.2017.04.019</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Zhang, Xinyu" sort="Zhang, Xinyu" uniqKey="Zhang X" first="Xinyu" last="Zhang">Xinyu Zhang</name></noRegion><name sortKey="Li, Chen" sort="Li, Chen" uniqKey="Li C" first="Chen" last="Li">Chen Li</name><name sortKey="Tan, Xianshi" sort="Tan, Xianshi" uniqKey="Tan X" first="Xianshi" last="Tan">Xianshi Tan</name><name sortKey="Wang, Hongfei" sort="Wang, Hongfei" uniqKey="Wang H" first="Hongfei" last="Wang">Hongfei Wang</name><name sortKey="Wang, Wenming" sort="Wang, Wenming" uniqKey="Wang W" first="Wenming" last="Wang">Wenming Wang</name><name sortKey="Wang, Zhuanhua" sort="Wang, Zhuanhua" uniqKey="Wang Z" first="Zhuanhua" last="Wang">Zhuanhua Wang</name><name sortKey="Wu, Lijie" sort="Wu, Lijie" uniqKey="Wu L" first="Lijie" last="Wu">Lijie Wu</name><name sortKey="Yuan, Hong" sort="Yuan, Hong" uniqKey="Yuan H" first="Hong" last="Yuan">Hong Yuan</name><name sortKey="Zhao, Yi" sort="Zhao, Yi" uniqKey="Zhao Y" first="Yi" last="Zhao">Yi Zhao</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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