Extraordinary μs-ms backbone dynamics in Arabidopsis thaliana peroxiredoxin Q.
Identifieur interne : 000948 ( Main/Exploration ); précédent : 000947; suivant : 000949Extraordinary μs-ms backbone dynamics in Arabidopsis thaliana peroxiredoxin Q.
Auteurs : Jörgen Adén [Suède] ; Marcus Wallgren ; Patrik Storm ; Christoph F. Weise ; Alexander Christiansen ; Wolfgang P. Schröder ; Christiane Funk ; Magnus Wolf-WatzSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2011.
Descripteurs français
- KwdFr :
- Arabidopsis (composition chimique), Arabidopsis (enzymologie), Arabidopsis (métabolisme), Modèles moléculaires (MeSH), Oxydoréduction (MeSH), Peroxirédoxines (analyse), Peroxirédoxines (composition chimique), Peroxirédoxines (isolement et purification), Peroxirédoxines (métabolisme), Pliage des protéines (MeSH), Protéines d'Arabidopsis (analyse), Protéines d'Arabidopsis (composition chimique), Protéines d'Arabidopsis (isolement et purification), Protéines d'Arabidopsis (métabolisme), Résonance magnétique nucléaire biomoléculaire (MeSH), Simulation de dynamique moléculaire (MeSH), Stabilité protéique (MeSH), Structure secondaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Température (MeSH), Thermodynamique (MeSH).
- MESH :
- analyse : Peroxirédoxines, Protéines d'Arabidopsis.
- composition chimique : Arabidopsis, Peroxirédoxines, Protéines d'Arabidopsis.
- enzymologie : Arabidopsis.
- isolement et purification : Peroxirédoxines, Protéines d'Arabidopsis.
- métabolisme : Arabidopsis, Peroxirédoxines, Protéines d'Arabidopsis.
- Modèles moléculaires, Oxydoréduction, Pliage des protéines, Résonance magnétique nucléaire biomoléculaire, Simulation de dynamique moléculaire, Stabilité protéique, Structure secondaire des protéines, Séquence d'acides aminés, Température, Thermodynamique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Arabidopsis (chemistry), Arabidopsis (enzymology), Arabidopsis (metabolism), Arabidopsis Proteins (analysis), Arabidopsis Proteins (chemistry), Arabidopsis Proteins (isolation & purification), Arabidopsis Proteins (metabolism), Models, Molecular (MeSH), Molecular Dynamics Simulation (MeSH), Nuclear Magnetic Resonance, Biomolecular (MeSH), Oxidation-Reduction (MeSH), Peroxiredoxins (analysis), Peroxiredoxins (chemistry), Peroxiredoxins (isolation & purification), Peroxiredoxins (metabolism), Protein Folding (MeSH), Protein Stability (MeSH), Protein Structure, Secondary (MeSH), Temperature (MeSH), Thermodynamics (MeSH).
- MESH :
- chemical , analysis : Arabidopsis Proteins, Peroxiredoxins.
- chemistry : Arabidopsis, Arabidopsis Proteins, Peroxiredoxins.
- enzymology : Arabidopsis.
- chemical , isolation & purification : Arabidopsis Proteins, Peroxiredoxins.
- metabolism : Arabidopsis, Arabidopsis Proteins, Peroxiredoxins.
- Amino Acid Sequence, Models, Molecular, Molecular Dynamics Simulation, Nuclear Magnetic Resonance, Biomolecular, Oxidation-Reduction, Protein Folding, Protein Stability, Protein Structure, Secondary, Temperature, Thermodynamics.
Abstract
Peroxiredoxin Q (PrxQ) isolated from Arabidopsis thaliana belongs to a family of redox enzymes called peroxiredoxins, which are thioredoxin- or glutaredoxin-dependent peroxidases acting to reduce peroxides and in particular hydrogen peroxide. PrxQ cycles between an active reduced state and an inactive oxidized state during its catalytic cycle. The catalytic mechanism involves a nucleophilic attack of the catalytic cysteine on hydrogen peroxide to generate a sulfonic acid intermediate with a concerted release of a water molecule. This intermediate is subsequently relaxed by the reaction of a second cysteine, denoted the resolving cysteine, generating an intramolecular disulfide bond and release of a second water molecule. PrxQ is recycled to the active state by a thioredoxin-dependent reduction. Previous structural studies of PrxQ homologues have provided the structural basis for the switch between reduced and oxidized conformations. Here, we have performed a detailed study of the activity, structure and dynamics of PrxQ in both the oxidized and reduced states. Reliable and experimentally validated structural models of PrxQ in both oxidation states were generated using homology based modeling. Analysis of NMR spin relaxation rates shows that PrxQ is monomeric in both oxidized and reduced states. As evident from R(2) relaxation rates the reduced form of PrxQ undergoes unprecedented dynamics on the slow μs-ms timescale. The ground state of this conformational dynamics is likely the stably folded reduced state as implied by circular dichroism spectroscopy. We speculate that the extensive dynamics is intimately related to the catalytic function of PrxQ.
DOI: 10.1016/j.bbapap.2011.07.011
PubMed: 21798375
Affiliations:
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Dynamics Simulation (MeSH)</term><term>Nuclear Magnetic Resonance, Biomolecular (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxiredoxins (analysis)</term><term>Peroxiredoxins (chemistry)</term><term>Peroxiredoxins (isolation & purification)</term><term>Peroxiredoxins (metabolism)</term><term>Protein Folding (MeSH)</term><term>Protein Stability (MeSH)</term><term>Protein Structure, Secondary (MeSH)</term><term>Temperature (MeSH)</term><term>Thermodynamics (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arabidopsis (composition chimique)</term><term>Arabidopsis (enzymologie)</term><term>Arabidopsis (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Peroxirédoxines (analyse)</term><term>Peroxirédoxines (composition chimique)</term><term>Peroxirédoxines (isolement et purification)</term><term>Peroxirédoxines (métabolisme)</term><term>Pliage des protéines (MeSH)</term><term>Protéines d'Arabidopsis 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xml:lang="en"><term>Amino Acid Sequence</term><term>Models, Molecular</term><term>Molecular Dynamics Simulation</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Oxidation-Reduction</term><term>Protein Folding</term><term>Protein Stability</term><term>Protein Structure, Secondary</term><term>Temperature</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Modèles moléculaires</term><term>Oxydoréduction</term><term>Pliage des protéines</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Simulation de dynamique moléculaire</term><term>Stabilité protéique</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term><term>Température</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Peroxiredoxin Q (PrxQ) isolated from Arabidopsis thaliana belongs to a family of redox enzymes called peroxiredoxins, which are thioredoxin- or glutaredoxin-dependent peroxidases acting to reduce peroxides and in particular hydrogen peroxide. PrxQ cycles between an active reduced state and an inactive oxidized state during its catalytic cycle. The catalytic mechanism involves a nucleophilic attack of the catalytic cysteine on hydrogen peroxide to generate a sulfonic acid intermediate with a concerted release of a water molecule. This intermediate is subsequently relaxed by the reaction of a second cysteine, denoted the resolving cysteine, generating an intramolecular disulfide bond and release of a second water molecule. PrxQ is recycled to the active state by a thioredoxin-dependent reduction. Previous structural studies of PrxQ homologues have provided the structural basis for the switch between reduced and oxidized conformations. Here, we have performed a detailed study of the activity, structure and dynamics of PrxQ in both the oxidized and reduced states. Reliable and experimentally validated structural models of PrxQ in both oxidation states were generated using homology based modeling. Analysis of NMR spin relaxation rates shows that PrxQ is monomeric in both oxidized and reduced states. As evident from R(2) relaxation rates the reduced form of PrxQ undergoes unprecedented dynamics on the slow μs-ms timescale. The ground state of this conformational dynamics is likely the stably folded reduced state as implied by circular dichroism spectroscopy. We speculate that the extensive dynamics is intimately related to the catalytic function of PrxQ.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21798375</PMID><DateCompleted><Year>2012</Year><Month>12</Month><Day>13</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1814</Volume><Issue>12</Issue><PubDate><Year>2011</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Extraordinary μs-ms backbone dynamics in Arabidopsis thaliana peroxiredoxin Q.</ArticleTitle><Pagination><MedlinePgn>1880-90</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbapap.2011.07.011</ELocationID><Abstract><AbstractText>Peroxiredoxin Q (PrxQ) isolated from Arabidopsis thaliana belongs to a family of redox enzymes called peroxiredoxins, which are thioredoxin- or glutaredoxin-dependent peroxidases acting to reduce peroxides and in particular hydrogen peroxide. PrxQ cycles between an active reduced state and an inactive oxidized state during its catalytic cycle. The catalytic mechanism involves a nucleophilic attack of the catalytic cysteine on hydrogen peroxide to generate a sulfonic acid intermediate with a concerted release of a water molecule. This intermediate is subsequently relaxed by the reaction of a second cysteine, denoted the resolving cysteine, generating an intramolecular disulfide bond and release of a second water molecule. PrxQ is recycled to the active state by a thioredoxin-dependent reduction. Previous structural studies of PrxQ homologues have provided the structural basis for the switch between reduced and oxidized conformations. Here, we have performed a detailed study of the activity, structure and dynamics of PrxQ in both the oxidized and reduced states. Reliable and experimentally validated structural models of PrxQ in both oxidation states were generated using homology based modeling. Analysis of NMR spin relaxation rates shows that PrxQ is monomeric in both oxidized and reduced states. As evident from R(2) relaxation rates the reduced form of PrxQ undergoes unprecedented dynamics on the slow μs-ms timescale. The ground state of this conformational dynamics is likely the stably folded reduced state as implied by circular dichroism spectroscopy. We speculate that the extensive dynamics is intimately related to the catalytic function of PrxQ.</AbstractText><CopyrightInformation>Copyright © 2011 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Adén</LastName><ForeName>Jörgen</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Umea University, Umea, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wallgren</LastName><ForeName>Marcus</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Storm</LastName><ForeName>Patrik</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Weise</LastName><ForeName>Christoph F</ForeName><Initials>CF</Initials></Author><Author ValidYN="Y"><LastName>Christiansen</LastName><ForeName>Alexander</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Schröder</LastName><ForeName>Wolfgang P</ForeName><Initials>WP</Initials></Author><Author ValidYN="Y"><LastName>Funk</LastName><ForeName>Christiane</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Wolf-Watz</LastName><ForeName>Magnus</ForeName><Initials>M</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><ArticleDate DateType="Electronic"><Year>2011</Year><Month>07</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029681">Arabidopsis Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="D054464">Peroxiredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="C510753">peroxiredoxin Q, Arabidopsis</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029681" MajorTopicYN="N">Arabidopsis Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D056004" MajorTopicYN="Y">Molecular Dynamics Simulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019906" MajorTopicYN="N">Nuclear Magnetic Resonance, Biomolecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055550" MajorTopicYN="N">Protein Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2011</Year><Month>04</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2011</Year><Month>06</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2011</Year><Month>07</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>7</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>7</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>12</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21798375</ArticleId><ArticleId IdType="pii">S1570-9639(11)00206-8</ArticleId><ArticleId IdType="doi">10.1016/j.bbapap.2011.07.011</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country></list><tree><noCountry><name sortKey="Christiansen, Alexander" sort="Christiansen, Alexander" uniqKey="Christiansen A" first="Alexander" last="Christiansen">Alexander Christiansen</name><name sortKey="Funk, Christiane" sort="Funk, Christiane" uniqKey="Funk C" first="Christiane" last="Funk">Christiane Funk</name><name sortKey="Schroder, Wolfgang P" sort="Schroder, Wolfgang P" uniqKey="Schroder W" first="Wolfgang P" last="Schröder">Wolfgang P. Schröder</name><name sortKey="Storm, Patrik" sort="Storm, Patrik" uniqKey="Storm P" first="Patrik" last="Storm">Patrik Storm</name><name sortKey="Wallgren, Marcus" sort="Wallgren, Marcus" uniqKey="Wallgren M" first="Marcus" last="Wallgren">Marcus Wallgren</name><name sortKey="Weise, Christoph F" sort="Weise, Christoph F" uniqKey="Weise C" first="Christoph F" last="Weise">Christoph F. Weise</name><name sortKey="Wolf Watz, Magnus" sort="Wolf Watz, Magnus" uniqKey="Wolf Watz M" first="Magnus" last="Wolf-Watz">Magnus Wolf-Watz</name></noCountry><country name="Suède"><noRegion><name sortKey="Aden, Jorgen" sort="Aden, Jorgen" uniqKey="Aden J" first="Jörgen" last="Adén">Jörgen Adén</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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