Conformational changes in redox pairs of protein structures
Identifieur interne : 000332 ( Ncbi/Merge ); précédent : 000331; suivant : 000333Conformational changes in redox pairs of protein structures
Auteurs : Samuel W. Fan ; Richard A. George ; Naomi L. Haworth ; Lina L. Feng ; Jason Y. Liu ; Merridee A. WoutersSource :
- Protein Science : A Publication of the Protein Society [ 0961-8368 ] ; 2009.
Abstract
Disulfides are conventionally viewed as structurally stabilizing elements in proteins but emerging evidence suggests two disulfide subproteomes exist. One group mediates the well known role of structural stabilization. A second redox‐active group are best known for their catalytic functions but are increasingly being recognized for their roles in regulation of protein function. Redox‐active disulfides are, by their very nature, more susceptible to reduction than structural disulfides; and conversely, the Cys pairs that form them are more susceptible to oxidation. In this study, we searched for potentially redox‐active Cys Pairs by scanning the Protein Data Bank for structures of proteins in alternate redox states. The PDB contains over 1134 unique redox pairs of proteins, many of which exhibit conformational differences between alternate redox states. Several classes of structural changes were observed, proteins that exhibit: disulfide oxidation following expulsion of metals such as zinc; major reorganisation of the polypeptide backbone in association with disulfide redox‐activity; order/disorder transitions; and changes in quaternary structure. Based on evidence gathered supporting disulfide redox activity, we propose disulfides present in alternate redox states are likely to have physiologically relevant redox activity.
Url:
DOI: 10.1002/pro.175
PubMed: 19598234
PubMed Central: 2776962
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<front><div type="abstract" xml:lang="en"><title>Abstract</title>
<p>Disulfides are conventionally viewed as structurally stabilizing elements in proteins but emerging evidence suggests two disulfide subproteomes exist. One group mediates the well known role of structural stabilization. A second redox‐active group are best known for their catalytic functions but are increasingly being recognized for their roles in regulation of protein function. Redox‐active disulfides are, by their very nature, more susceptible to reduction than structural disulfides; and conversely, the Cys pairs that form them are more susceptible to oxidation. In this study, we searched for potentially redox‐active Cys Pairs by scanning the Protein Data Bank for structures of proteins in alternate redox states. The PDB contains over 1134 unique redox pairs of proteins, many of which exhibit conformational differences between alternate redox states. Several classes of structural changes were observed, proteins that exhibit: disulfide oxidation following expulsion of metals such as zinc; major reorganisation of the polypeptide backbone in association with disulfide redox‐activity; order/disorder transitions; and changes in quaternary structure. Based on evidence gathered supporting disulfide redox activity, we propose disulfides present in alternate redox states are likely to have physiologically relevant redox activity.</p>
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<title-group><article-title>Conformational changes in redox pairs of protein structures</article-title>
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<contrib-group><contrib id="au1" contrib-type="author"><name><surname>Fan</surname>
<given-names>Samuel W.</given-names>
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<xref ref-type="aff" rid="af1"><sup>1</sup>
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<xref ref-type="aff" rid="af2"><sup>2</sup>
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<xref ref-type="author-notes" rid="fn2"><sup>†</sup>
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<contrib id="au2" contrib-type="author"><name><surname>George</surname>
<given-names>Richard A.</given-names>
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<xref ref-type="aff" rid="af1"><sup>1</sup>
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<xref ref-type="author-notes" rid="fn2"><sup>†</sup>
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<contrib id="au3" contrib-type="author"><name><surname>Haworth</surname>
<given-names>Naomi L.</given-names>
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<xref ref-type="aff" rid="af1"><sup>1</sup>
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<contrib id="au4" contrib-type="author"><name><surname>Feng</surname>
<given-names>Lina L.</given-names>
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<xref ref-type="aff" rid="af1"><sup>1</sup>
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<contrib id="au5" contrib-type="author"><name><surname>Liu</surname>
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<contrib id="au6" contrib-type="author" corresp="yes"><name><surname>Wouters</surname>
<given-names>Merridee A.</given-names>
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<xref ref-type="aff" rid="af2"><sup>2</sup>
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<address><email>m.wouters@victorchang.edu.au</email>
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<aff id="af1"><label><sup>1</sup>
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Structural and Computational Biology Program, Victor Chang Cardiac Research Institute, Darlinghurst, New South Wales 2010, Australia</aff>
<aff id="af2"><label><sup>2</sup>
</label>
School of Medical Sciences, University of New South Wales, New South Wales 2052, Australia</aff>
<author-notes><corresp id="correspondenceTo"><label>*</label>
Structural and Computational Biology Program, Victor Chang Cardiac Research Institute, 405 Liverpool St, Darlinghurst, 2010, Sydney, NSW, Australia</corresp>
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<p>Samuel W. Fan and Richard A. George contributed equally to this work.</p>
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<pub-date pub-type="epub"><day>28</day>
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<permissions><copyright-statement content-type="article-copyright">Copyright © 2009 The Protein Society</copyright-statement>
<license><license-p>This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.</license-p>
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<abstract><title>Abstract</title>
<p>Disulfides are conventionally viewed as structurally stabilizing elements in proteins but emerging evidence suggests two disulfide subproteomes exist. One group mediates the well known role of structural stabilization. A second redox‐active group are best known for their catalytic functions but are increasingly being recognized for their roles in regulation of protein function. Redox‐active disulfides are, by their very nature, more susceptible to reduction than structural disulfides; and conversely, the Cys pairs that form them are more susceptible to oxidation. In this study, we searched for potentially redox‐active Cys Pairs by scanning the Protein Data Bank for structures of proteins in alternate redox states. The PDB contains over 1134 unique redox pairs of proteins, many of which exhibit conformational differences between alternate redox states. Several classes of structural changes were observed, proteins that exhibit: disulfide oxidation following expulsion of metals such as zinc; major reorganisation of the polypeptide backbone in association with disulfide redox‐activity; order/disorder transitions; and changes in quaternary structure. Based on evidence gathered supporting disulfide redox activity, we propose disulfides present in alternate redox states are likely to have physiologically relevant redox activity.</p>
</abstract>
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<tree><noCountry><name sortKey="Fan, Samuel W" sort="Fan, Samuel W" uniqKey="Fan S" first="Samuel W." last="Fan">Samuel W. Fan</name>
<name sortKey="Feng, Lina L" sort="Feng, Lina L" uniqKey="Feng L" first="Lina L." last="Feng">Lina L. Feng</name>
<name sortKey="George, Richard A" sort="George, Richard A" uniqKey="George R" first="Richard A." last="George">Richard A. George</name>
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<name sortKey="Liu, Jason Y" sort="Liu, Jason Y" uniqKey="Liu J" first="Jason Y." last="Liu">Jason Y. Liu</name>
<name sortKey="Wouters, Merridee A" sort="Wouters, Merridee A" uniqKey="Wouters M" first="Merridee A." last="Wouters">Merridee A. Wouters</name>
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