Crystal structure of XMRV protease differs from the structures of other retropepsins
Identifieur interne : 001A01 ( Istex/Corpus ); précédent : 001A00; suivant : 001A02Crystal structure of XMRV protease differs from the structures of other retropepsins
Auteurs : Mi Li ; Frank Dimaio ; Dongwen Zhou ; Alla Gustchina ; Jacek Lubkowski ; Zbigniew Dauter ; David Baker ; Alexander WlodawerSource :
- Nature Structural & Molecular Biology [ 1545-9993 ] ; 2011-02.
Abstract
XMRV is a retrovirus that has been linked to prostate cancer and chronic fatigue syndrome. The crystal structure of the XMRV protease differs from the structures of other retropepsins and instead resembles those of pepsin-like enzymes, suggesting that this protease may represent a distinct evolutionary branch of the aspartic proteases.
Url:
DOI: 10.1038/nsmb.1964
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<ref target="http://www.tei-c.org/">We use TEI</ref></desc></application></appInfo></encodingDesc><profileDesc><abstract><p>Using energy and density guided Rosetta refinement to improve molecular replacement, we determined the crystal structure of the protease encoded by xenotropic murine leukemia virus–related virus (XMRV). Despite overall similarity of <rs>XMRV protease</rs> to other retropepsins, the topology of its dimer interface more closely resembles those of the monomeric, pepsin-like enzymes. 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All Rights Reserved.</cpn></cpg><suppinfo id="S1"><suppobj extrefid="nsmb.1964-S1" format="pdf" filesize="3M"><title>Supplementary Text and Figures</title><descrip><p>Supplementary Figures 1–7, Supplementary Tables 1 and 2, and Supplementary Methods</p></descrip></suppobj></suppinfo><subject code="npg_subject_474"></subject><doi>10.1038/nsmb.1964</doi></pubfm><fm><atl>Crystal structure of <named-entity id="named-entity-1">XMRV protease</named-entity> differs from the structures of other retropepsins</atl><aug><au><fnm>Mi</fnm><snm>Li</snm><inits>M</inits><orf rid="a1"></orf><orf rid="a2"></orf></au><au><fnm>Frank</fnm><snm>DiMaio</snm><inits>F</inits><orf rid="a3"></orf></au><au><fnm>Dongwen</fnm><snm>Zhou</snm><inits>D</inits><orf rid="a1"></orf></au><au><fnm>Alla</fnm><snm>Gustchina</snm><inits>A</inits><orf rid="a1"></orf></au><au><fnm>Jacek</fnm><snm>Lubkowski</snm><inits>J</inits><orf rid="a4"></orf></au><au><fnm>Zbigniew</fnm><snm>Dauter</snm><inits>Z</inits><orf rid="a5"></orf></au><au><fnm>David</fnm><snm>Baker</snm><inits>D</inits><orf rid="a3"></orf></au><cau><fnm>Alexander</fnm><snm>Wlodawer</snm><inits>A</inits><orf rid="a1"></orf><corf rid="c1"></corf></cau><aff><oid id="a1"></oid><org>Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick</org>, <cty>Frederick</cty>, <st>Maryland</st>, <cny>USA</cny>.</aff><aff><oid id="a2"></oid><org>Basic Research Program, SAIC-Frederick</org>, <cty>Frederick</cty>, <st>Maryland</st>, <cny>USA</cny>.</aff><aff><oid id="a3"></oid><org>Department of Biochemistry, University of Washington</org>, <cty>Seattle</cty>, <st>Washington</st>, <cny>USA</cny>.</aff><aff><oid id="a4"></oid><org>Macromolecular Assembly Structure and Cell Signaling Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick</org>, <cty>Frederick</cty>, <st>Maryland</st>, <cny>USA</cny>.</aff><aff><oid id="a5"></oid><org>Synchrotron Radiation Research Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Argonne National Laboratory</org>, <cty>Argonne</cty>, <st>Illinois</st>, <cny>USA</cny>.</aff><caff><coid id="c1"></coid><email>wlodawer@nih.gov</email></caff></aug><hst><re year="2010" month="07" day="29"></re><acc year="2010" month="10" day="29"></acc><pubdate type="aop" year="2011" month="01" day="23"></pubdate></hst><edsumm type="standfirst" publish="aop"><title></title><p>XMRV is a retrovirus that has been linked to prostate cancer and chronic fatigue syndrome. The crystal structure of the XMRV protease differs from the structures of other retropepsins and instead resembles those of pepsin-like enzymes, suggesting that this protease may represent a distinct evolutionary branch of the aspartic proteases.</p></edsumm><edsumm type="standfirst" publish="issue"><title></title><p>XMRV is a retrovirus that has been linked to prostate cancer and chronic fatigue syndrome. The crystal structure of the XMRV protease differs from the structures of other retropepsins and instead resembles those of pepsin-like enzymes, suggesting that this protease may represent a distinct evolutionary branch of the aspartic proteases.</p></edsumm></fm></article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="eng"><title>Crystal structure of XMRV protease differs from the structures of other retropepsins</title></titleInfo><titleInfo type="alternative" lang="eng" contentType="CDATA"><title>Crystal structure of XMRV protease differs from the structures of other retropepsins</title></titleInfo><name type="personal"><namePart type="given">Mi</namePart><namePart type="family">Li</namePart><affiliation>Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, Maryland, USA.</affiliation><affiliation>Basic Research Program, SAIC-Frederick, Frederick, Maryland, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Frank</namePart><namePart type="family">DiMaio</namePart><affiliation>Department of Biochemistry, University of Washington, Seattle, Washington, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Dongwen</namePart><namePart type="family">Zhou</namePart><affiliation>Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, Maryland, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Alla</namePart><namePart type="family">Gustchina</namePart><affiliation>Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, Maryland, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jacek</namePart><namePart type="family">Lubkowski</namePart><affiliation>Macromolecular Assembly Structure and Cell Signaling Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, Maryland, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Zbigniew</namePart><namePart type="family">Dauter</namePart><affiliation>Synchrotron Radiation Research Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Argonne National Laboratory, Argonne, Illinois, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">David</namePart><namePart type="family">Baker</namePart><affiliation>Department of Biochemistry, University of Washington, Seattle, Washington, USA.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Alexander</namePart><namePart type="family">Wlodawer</namePart><affiliation>Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, Maryland, USA.</affiliation><affiliation>E-mail: wlodawer@nih.gov</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Brief Communications (bc)" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.</publisher><dateIssued encoding="w3cdtf">2011-02</dateIssued><dateCaptured encoding="w3cdtf">2010-07-29</dateCaptured><dateValid encoding="w3cdtf">2010-10-29</dateValid><copyrightDate encoding="w3cdtf">2011</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract type="editorial-summary" lang="eng">XMRV is a retrovirus that has been linked to prostate cancer and chronic fatigue syndrome. The crystal structure of the XMRV protease differs from the structures of other retropepsins and instead resembles those of pepsin-like enzymes, suggesting that this protease may represent a distinct evolutionary branch of the aspartic proteases.</abstract><note type="additional-physical-form">Supplementary Text and Figures : Supplementary Figures 1–7, Supplementary Tables 1 and 2, and Supplementary Methods [nsmb.1964-S1]</note><relatedItem type="host"><titleInfo><title>Nature Structural & Molecular Biology</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><subject displayLabel="npg_subject_474"><genre>category</genre><topic>npg_subject_474</topic></subject><identifier type="ISSN">1545-9993</identifier><identifier type="eISSN">1545-9985</identifier><part><date>2011</date><detail type="volume"><caption>vol.</caption><number>18</number></detail><detail type="issue"><caption>no.</caption><number>2</number></detail><extent unit="pages"><start>227</start><end>229</end><total>3</total></extent></part></relatedItem><relatedItem type="references" displayLabel="b1"><titleInfo><title>Proc. 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|texte= Crystal structure of XMRV protease differs from the structures of other retropepsins
}}
| This area was generated with Dilib version V0.6.33. |  |