Coiled‐coil deformations in crystal structures: the measles virus phosphoprotein multimerization domain as an illustrative example
Identifieur interne : 002431 ( Istex/Corpus ); précédent : 002430; suivant : 002432Coiled‐coil deformations in crystal structures: the measles virus phosphoprotein multimerization domain as an illustrative example
Auteurs : David Blocquel ; Johnny Habchi ; Eric Durand ; Marion Sevajol ; François Ferron ; Jenny Erales ; Nicolas Papageorgiou ; Sonia LonghiSource :
- Acta Crystallographica Section D [ 1399-0047 ] ; 2014-06-01.
Abstract
The structures of two constructs of the measles virus (MeV) phosphoprotein (P) multimerization domain (PMD) are reported and are compared with a third structure published recently by another group [Communie et al. (2013), J. Virol.87, 7166–7169]. Although the three structures all have a tetrameric and parallel coiled‐coil arrangement, structural comparison unveiled considerable differences in the quaternary structure and unveiled that the three structures suffer from significant structural deformation induced by intermolecular interactions within the crystal. These results show that crystal packing can bias conclusions about function and mechanism based on analysis of a single crystal structure, and they challenge to some extent the assumption according to which coiled‐coil structures can be reliably predicted from the amino‐acid sequence. Structural comparison also highlighted significant differences in the extent of disorder in the C‐terminal region of each monomer. The differential flexibility of the C‐terminal region is also supported by size‐exclusion chromatography and small‐angle X‐ray scattering studies, which showed that MeV PMD exists in solution as a dynamic equilibrium between two tetramers of different compaction. Finally, the possible functional implications of the flexibility of the C‐terminal region of PMD are discussed.
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DOI: 10.1107/S139900471400234X
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(2013), J. Virol.87, 7166–7169]. Although the three structures all have a tetrameric and parallel coiled‐coil arrangement, structural comparison unveiled considerable differences in the quaternary structure and unveiled that the three structures suffer from significant structural deformation induced by intermolecular interactions within the crystal. These results show that crystal packing can bias conclusions about function and mechanism based on analysis of a single crystal structure, and they challenge to some extent the assumption according to which coiled‐coil structures can be reliably predicted from the amino‐acid sequence. Structural comparison also highlighted significant differences in the extent of disorder in the C‐terminal region of each monomer. The differential flexibility of the C‐terminal region is also supported by size‐exclusion chromatography and small‐angle X‐ray scattering studies, which showed that MeV PMD exists in solution as a dynamic equilibrium between two tetramers of different compaction. 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These results show that crystal packing can bias conclusions about function and mechanism based on analysis of a single crystal structure, and they challenge to some extent the assumption according to which coiled‐coil structures can be reliably predicted from the amino‐acid sequence. Structural comparison also highlighted significant differences in the extent of disorder in the C‐terminal region of each monomer. The differential flexibility of the C‐terminal region is also supported by size‐exclusion chromatography and small‐angle X‐ray scattering studies, which showed that MeV PMD exists in solution as a dynamic equilibrium between two tetramers of different compaction. Finally, the possible functional implications of the flexibility of the C‐terminal region of PMD are discussed.</p></abstract><textClass><keywords xml:lang="en"><term xml:id="k1">coiled coils</term><term xml:id="k2"><hi rend="italic">measles virus</hi> phosphoprotein multimerization domain</term></keywords><keywords rend="tocHeading1"><term>research papers</term></keywords></textClass><langUsage><language ident="en"></language></langUsage></profileDesc><revisionDesc><change when="2019-12-20" who="#istex" xml:id="pub2tei">formatting</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-4R7TNZSX-3/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>International Union of Crystallography</publisherName><publisherLoc>5 Abbey Square, Chester, Cheshire CH1 2HU, England</publisherLoc></publisherInfo><doi origin="wiley" registered="yes">10.1111/(ISSN)1399-0047</doi><issn type="print">1399-0047</issn><issn type="electronic">1399-0047</issn><idGroup><id type="product" value="AYD2"></id></idGroup><titleGroup><title type="main" sort="ACTA CRYSTALLOGRAPHICA D">Acta Crystallographica Section D</title><title type="short">Acta Crystallographica D</title></titleGroup></publicationMeta><publicationMeta level="part" position="06106"><doi origin="wiley">10.1111/ayd2.2014.70.issue-6</doi><numberingGroup><numbering type="journalVolume" number="70">70</numbering><numbering type="journalIssue" number="6">6</numbering></numberingGroup><coverDate startDate="2014-06-01">June 2014</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="10" status="forIssue"><doi origin="wiley">10.1107/S139900471400234X</doi><idGroup><id type="unit" value="AYD2DZ5322"></id><id type="society" value="dz5322"></id></idGroup><titleGroup><title type="tocHeading1">research papers</title></titleGroup><copyright>International Union of Crystallography, 2014</copyright><eventGroup><event type="xmlConverted" agent="Converter:BPG_TO_WML3G version:3.3.2 mode:FullText" date="2014-06-26"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.3.2 mode:FullText" date="2014-06-26"></event><event type="firstOnline" date="2014-06-26"></event><event type="publishedOnlineFinalForm" date="2014-06-26"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.6.4 mode:FullText" date="2015-10-07"></event></eventGroup><numberingGroup><numbering type="pageFirst" number="1589">1589</numbering><numbering type="pageLast" number="1603">1603</numbering></numberingGroup><correspondenceTo>Nicolas Papageorgiou, e‐mail: <email normalForm="nicolas.papageorgiou@afmb.univ-mrs.fr">nicolas.papageorgiou@afmb.univ‐mrs.fr</email>; Sonia Longhi, e‐mail: <email normalForm="sonia.longhi@afmb.univ-mrs.fr">sonia.longhi@afmb.univ‐mrs.fr</email></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:AYD2.AYD2DZ5322.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>Received 9 January 2014, accepted 31 January 2014</unparsedEditorialHistory><countGroup><count type="figureTotal" number="0"></count><count type="tableTotal" number="0"></count><count type="formulaTotal" number="0"></count><count type="wordTotal" number="0"></count><count type="referenceTotal" number="0"></count><count type="linksCrossRef" number="0"></count><count type="linksPubMed" number="0"></count></countGroup><titleGroup><title type="main">Coiled‐coil deformations in crystal structures: the <i>measles virus</i> phosphoprotein multimerization domain as an illustrative example</title><title type="short">Coiled‐coil deformations</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1"><personName><givenNames>David</givenNames><familyName>Blocquel</familyName></personName></creator><creator creatorRole="author" xml:id="cr2"><personName><givenNames>Johnny</givenNames><familyName>Habchi</familyName></personName></creator><creator creatorRole="author" xml:id="cr3"><personName><givenNames>Eric</givenNames><familyName>Durand</familyName></personName></creator><creator creatorRole="author" xml:id="cr4"><personName><givenNames>Marion</givenNames><familyName>Sevajol</familyName></personName></creator><creator creatorRole="author" xml:id="cr5"><personName><givenNames>François</givenNames><familyName>Ferron</familyName></personName></creator><creator creatorRole="author" xml:id="cr6"><personName><givenNames>Jenny</givenNames><familyName>Erales</familyName></personName></creator><creator creatorRole="author" xml:id="cr7"><personName><givenNames>Nicolas</givenNames><familyName>Papageorgiou</familyName></personName></creator><creator creatorRole="author" xml:id="cr8"><personName><givenNames>Sonia</givenNames><familyName>Longhi</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="a1" countryCode="FR"><unparsedAffiliation>Aix‐Marseille University, AFMB UMR 7257, 13288 Marseille, France</unparsedAffiliation></affiliation><affiliation xml:id="a2" countryCode="FR"><unparsedAffiliation>CNRS, AFMB UMR 7257, 13288 Marseille, France</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en"><keyword xml:id="k1">coiled coils</keyword><keyword xml:id="k2"><i>measles virus</i> phosphoprotein multimerization domain</keyword></keywordGroup><supportingInformation><p>PDB reference: <link href="http://scripts.iucr.org/cgi-bin/cr.cgi?rm=pdb&pdbId=4bhv">
measles virus phosphoprotein multimerization domain, 4bhv</link></p><p>PDB reference: <link href="http://scripts.iucr.org/cgi-bin/cr.cgi?rm=pdb&pdbId=4c5q">
4c5q</link></p><p>Supporting Information. DOI: <link href="http://dx.doi.org/10.1107/S139900471400234X/dz5322sup1.pdf">10.1107/S139900471400234X/dz5322sup1.pdf</link></p><p>Supplementary Movie S1. DOI: <link href="http://dx.doi.org/10.1107/S139900471400234X/dz5322sup2.avi">10.1107/S139900471400234X/dz5322sup2.avi</link></p><p>Supplementary Movie S2. DOI: <link href="http://dx.doi.org/10.1107/S139900471400234X/dz5322sup3.avi">10.1107/S139900471400234X/dz5322sup3.avi</link></p><p>Supplementary Movie S3. DOI: <link href="http://dx.doi.org/10.1107/S139900471400234X/dz5322sup4.avi">10.1107/S139900471400234X/dz5322sup4.avi</link></p></supportingInformation><abstractGroup><abstract type="main" xml:lang="en"><p>The structures of two constructs of the <i>measles virus</i> (MeV) phosphoprotein (P) multimerization domain (PMD) are reported and are compared with a third structure published recently by another group [Communie <i>et al.</i> (2013), <i>J. Virol.</i><b>87</b>, 7166–7169]. Although the three structures all have a tetrameric and parallel coiled‐coil arrangement, structural comparison unveiled considerable differences in the quaternary structure and unveiled that the three structures suffer from significant structural deformation induced by intermolecular interactions within the crystal. These results show that crystal packing can bias conclusions about function and mechanism based on analysis of a single crystal structure, and they challenge to some extent the assumption according to which coiled‐coil structures can be reliably predicted from the amino‐acid sequence. Structural comparison also highlighted significant differences in the extent of disorder in the C‐terminal region of each monomer. The differential flexibility of the C‐terminal region is also supported by size‐exclusion chromatography and small‐angle X‐ray scattering studies, which showed that MeV PMD exists in solution as a dynamic equilibrium between two tetramers of different compaction. Finally, the possible functional implications of the flexibility of the C‐terminal region of PMD are discussed.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Coiled‐coil deformations in crystal structures: the measles virus phosphoprotein multimerization domain as an illustrative example</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Coiled‐coil deformations</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Coiled‐coil deformations in crystal structures: the measles virus phosphoprotein multimerization domain as an illustrative example</title></titleInfo><name type="personal"><namePart type="given">David</namePart><namePart type="family">Blocquel</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Johnny</namePart><namePart type="family">Habchi</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Eric</namePart><namePart type="family">Durand</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Marion</namePart><namePart type="family">Sevajol</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">François</namePart><namePart type="family">Ferron</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jenny</namePart><namePart type="family">Erales</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Nicolas</namePart><namePart type="family">Papageorgiou</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Sonia</namePart><namePart type="family">Longhi</namePart><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>International Union of Crystallography</publisher><place><placeTerm type="text">5 Abbey Square, Chester, Cheshire CH1 2HU, England</placeTerm></place><dateIssued encoding="w3cdtf">2014-06-01</dateIssued><edition>Received 9 January 2014, accepted 31 January 2014</edition><copyrightDate encoding="w3cdtf">2014</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="figures">0</extent><extent unit="tables">0</extent><extent unit="formulas">0</extent><extent unit="references">0</extent><extent unit="linksCrossRef">0</extent><extent unit="words">0</extent></physicalDescription><abstract lang="en">The structures of two constructs of the measles virus (MeV) phosphoprotein (P) multimerization domain (PMD) are reported and are compared with a third structure published recently by another group [Communie et al. (2013), J. Virol.87, 7166–7169]. Although the three structures all have a tetrameric and parallel coiled‐coil arrangement, structural comparison unveiled considerable differences in the quaternary structure and unveiled that the three structures suffer from significant structural deformation induced by intermolecular interactions within the crystal. These results show that crystal packing can bias conclusions about function and mechanism based on analysis of a single crystal structure, and they challenge to some extent the assumption according to which coiled‐coil structures can be reliably predicted from the amino‐acid sequence. Structural comparison also highlighted significant differences in the extent of disorder in the C‐terminal region of each monomer. The differential flexibility of the C‐terminal region is also supported by size‐exclusion chromatography and small‐angle X‐ray scattering studies, which showed that MeV PMD exists in solution as a dynamic equilibrium between two tetramers of different compaction. Finally, the possible functional implications of the flexibility of the C‐terminal region of PMD are discussed.</abstract><subject lang="en"><genre>keywords</genre><topic>coiled coils</topic><topic>measles virus phosphoprotein multimerization domain</topic></subject><relatedItem type="host"><titleInfo><title>Acta Crystallographica Section D</title></titleInfo><titleInfo type="abbreviated"><title>Acta Crystallographica D</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><note type="content"> PDB reference: measles virus phosphoprotein multimerization domain, 4bhv PDB reference: 4c5q Supporting Information. DOI: 10.1107/S139900471400234X/dz5322sup1.pdf Supplementary Movie S1. DOI: 10.1107/S139900471400234X/dz5322sup2.avi Supplementary Movie S2. DOI: 10.1107/S139900471400234X/dz5322sup3.avi Supplementary Movie S3. DOI: 10.1107/S139900471400234X/dz5322sup4.avi PDB reference: measles virus phosphoprotein multimerization domain, 4bhv PDB reference: 4c5q Supporting Information. DOI: 10.1107/S139900471400234X/dz5322sup1.pdf Supplementary Movie S1. DOI: 10.1107/S139900471400234X/dz5322sup2.avi Supplementary Movie S2. DOI: 10.1107/S139900471400234X/dz5322sup3.avi Supplementary Movie S3. DOI: 10.1107/S139900471400234X/dz5322sup4.avi PDB reference: measles virus phosphoprotein multimerization domain, 4bhv PDB reference: 4c5q Supporting Information. DOI: 10.1107/S139900471400234X/dz5322sup1.pdf Supplementary Movie S1. DOI: 10.1107/S139900471400234X/dz5322sup2.avi Supplementary Movie S2. DOI: 10.1107/S139900471400234X/dz5322sup3.avi Supplementary Movie S3. DOI: 10.1107/S139900471400234X/dz5322sup4.avi PDB reference: measles virus phosphoprotein multimerization domain, 4bhv PDB reference: 4c5q Supporting Information. DOI: 10.1107/S139900471400234X/dz5322sup1.pdf Supplementary Movie S1. DOI: 10.1107/S139900471400234X/dz5322sup2.avi Supplementary Movie S2. DOI: 10.1107/S139900471400234X/dz5322sup3.avi Supplementary Movie S3. DOI: 10.1107/S139900471400234X/dz5322sup4.avi PDB reference: measles virus phosphoprotein multimerization domain, 4bhv PDB reference: 4c5q Supporting Information. DOI: 10.1107/S139900471400234X/dz5322sup1.pdf Supplementary Movie S1. DOI: 10.1107/S139900471400234X/dz5322sup2.avi Supplementary Movie S2. DOI: 10.1107/S139900471400234X/dz5322sup3.avi Supplementary Movie S3. DOI: 10.1107/S139900471400234X/dz5322sup4.avi PDB reference: measles virus phosphoprotein multimerization domain, 4bhv PDB reference: 4c5q Supporting Information. DOI: 10.1107/S139900471400234X/dz5322sup1.pdf Supplementary Movie S1. DOI: 10.1107/S139900471400234X/dz5322sup2.avi Supplementary Movie S2. DOI: 10.1107/S139900471400234X/dz5322sup3.avi Supplementary Movie S3. DOI: 10.1107/S139900471400234X/dz5322sup4.avi</note><identifier type="ISSN">1399-0047</identifier><identifier type="eISSN">1399-0047</identifier><identifier type="DOI">10.1111/(ISSN)1399-0047</identifier><identifier type="PublisherID">AYD2</identifier><part><date>2014</date><detail type="volume"><caption>vol.</caption><number>70</number></detail><detail type="issue"><caption>no.</caption><number>6</number></detail><extent unit="pages"><start>1589</start><end>1603</end></extent></part></relatedItem><identifier type="istex">44EACFF55766D71111B39E072C2056765063F778</identifier><identifier type="ark">ark:/67375/WNG-4R7TNZSX-3</identifier><identifier type="DOI">10.1107/S139900471400234X</identifier><identifier type="ArticleID">AYD2DZ5322</identifier><accessCondition type="use and reproduction" contentType="copyright">International Union of Crystallography, 2014</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-L0C46X92-X">wiley</recordContentSource><recordOrigin>Converted from (version ) to MODS version 3.6.</recordOrigin><recordCreationDate encoding="w3cdtf">2019-11-13</recordCreationDate></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-4R7TNZSX-3/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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