Crystallization of a proteolyzed form of the horse pancreatic lipase‐related protein 2: structural basis for the specific detergent requirement
Identifieur interne : 000736 ( Istex/Corpus ); précédent : 000735; suivant : 000737Crystallization of a proteolyzed form of the horse pancreatic lipase‐related protein 2: structural basis for the specific detergent requirement
Auteurs : José M. Manche O ; Sandrine Jayne ; Brigritte Kerfelec ; Catherine Chapus ; Isabelle Crenon ; Juan A. HermosoSource :
- Acta Crystallographica Section D [ 1399-0047 ] ; 2004-11.
English descriptors
- KwdEn :
Abstract
Horse pancreatic lipase‐related proteins PLRP1 and PLRP2 are produced by the pancreas together with pancreatic lipase (PL). Sequence‐comparison analyses reveal that the three proteins possess the same two‐domain organization: an N‐terminal catalytic domain and a C‐terminal domain, which in PL is involved in colipase binding. Nevertheless, despite the high level of sequence identity found, they exhibit distinct enzymatic properties. The intrinsic sensitivity of the peptide bond between Ser245 and Thr246 within the flap region of PLRP2 to proteolytic cleavage probably complicates PLRP2 crystallization since, as shown here, this proteolyzed form of PLRP2 is only crystallized after specific detergent stabilization of this region. This has been performed by the hanging‐drop vapour‐diffusion method at 291 K and exclusively in the presence of N,N‐dimethyldecylamine‐β‐oxide (DDAO). However, most crystals (>95%) are highly twinned and diffract poorly (to ∼7–5 Å resolution). Diffraction‐quality trigonal crystals have unit‐cell parameters a = b = 128.4, c = 85.8 Å and belong to space group P3221. A 2.9 Å native data set was collected at ESRF on beamline ID14‐2 with an Rmerge of 12.7%. Preliminary structural analysis provides a structural basis for the specific roles of DDAO.
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DOI: 10.1107/S0907444904024229
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Sequence‐comparison analyses reveal that the three proteins possess the same two‐domain organization: an N‐terminal catalytic domain and a C‐terminal domain, which in PL is involved in colipase binding. Nevertheless, despite the high level of sequence identity found, they exhibit distinct enzymatic properties. The intrinsic sensitivity of the peptide bond between Ser245 and Thr246 within the flap region of PLRP2 to proteolytic cleavage probably complicates PLRP2 crystallization since, as shown here, this proteolyzed form of PLRP2 is only crystallized after specific detergent stabilization of this region. This has been performed by the hanging‐drop vapour‐diffusion method at 291 K and exclusively in the presence of N,N‐dimethyldecylamine‐β‐oxide (DDAO). However, most crystals (>95%) are highly twinned and diffract poorly (to ∼7–5 Å resolution). Diffraction‐quality trigonal crystals have unit‐cell parameters a = b = 128.4, c = 85.8 Å and belong to space group P3221. A 2.9 Å native data set was collected at ESRF on beamline ID14‐2 with an Rmerge of 12.7%. Preliminary structural analysis provides a structural basis for the specific roles of DDAO.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>José M. Mancheño</name><affiliations><json:string>Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain</json:string><json:string>INSERM‐U476 Nutrition Humaine et Lipides, 18 Avenue Mozart, 13009 Marseille, France</json:string></affiliations></json:item><json:item><name>Sandrine Jayne</name><affiliations><json:string>Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain</json:string><json:string>INSERM‐U476 Nutrition Humaine et Lipides, 18 Avenue Mozart, 13009 Marseille, France</json:string></affiliations></json:item><json:item><name>Brigritte Kerfelec</name><affiliations><json:string>Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain</json:string><json:string>INSERM‐U476 Nutrition Humaine et Lipides, 18 Avenue Mozart, 13009 Marseille, France</json:string></affiliations></json:item><json:item><name>Catherine Chapus</name><affiliations><json:string>Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain</json:string><json:string>INSERM‐U476 Nutrition Humaine et Lipides, 18 Avenue Mozart, 13009 Marseille, France</json:string></affiliations></json:item><json:item><name>Isabelle Crenon</name><affiliations><json:string>Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain</json:string><json:string>INSERM‐U476 Nutrition Humaine et Lipides, 18 Avenue Mozart, 13009 Marseille, France</json:string></affiliations></json:item><json:item><name>Juan A. Hermoso</name><affiliations><json:string>Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain</json:string><json:string>INSERM‐U476 Nutrition Humaine et Lipides, 18 Avenue Mozart, 13009 Marseille, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>detergent</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>lipase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>flap stabilization.</value></json:item></subject><language><json:string>eng</json:string></language><abstract>Horse pancreatic lipase‐related proteins PLRP1 and PLRP2 are produced by the pancreas together with pancreatic lipase (PL). Sequence‐comparison analyses reveal that the three proteins possess the same two‐domain organization: an N‐terminal catalytic domain and a C‐terminal domain, which in PL is involved in colipase binding. Nevertheless, despite the high level of sequence identity found, they exhibit distinct enzymatic properties. The intrinsic sensitivity of the peptide bond between Ser245 and Thr246 within the flap region of PLRP2 to proteolytic cleavage probably complicates PLRP2 crystallization since, as shown here, this proteolyzed form of PLRP2 is only crystallized after specific detergent stabilization of this region. This has been performed by the hanging‐drop vapour‐diffusion method at 291 K and exclusively in the presence of N,N‐dimethyldecylamine‐β‐oxide (DDAO). However, most crystals (>95%) are highly twinned and diffract poorly (to ∼7–5 Å resolution). Diffraction‐quality trigonal crystals have unit‐cell parameters a = b = 128.4, c = 85.8 Å and belong to space group P3221. A 2.9 Å native data set was collected at ESRF on beamline ID14‐2 with an Rmerge of 12.7%. 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Sequence‐comparison analyses reveal that the three proteins possess the same two‐domain organization: an N‐terminal catalytic domain and a C‐terminal domain, which in PL is involved in colipase binding. Nevertheless, despite the high level of sequence identity found, they exhibit distinct enzymatic properties. The intrinsic sensitivity of the peptide bond between Ser245 and Thr246 within the flap region of PLRP2 to proteolytic cleavage probably complicates PLRP2 crystallization since, as shown here, this proteolyzed form of PLRP2 is only crystallized after specific detergent stabilization of this region. This has been performed by the hanging‐drop vapour‐diffusion method at 291 K and exclusively in the presence of N,N‐dimethyldecylamine‐β‐oxide (DDAO). However, most crystals (>95%) are highly twinned and diffract poorly (to ∼7–5 Å resolution). Diffraction‐quality trigonal crystals have unit‐cell parameters a = b = 128.4, c = 85.8 Å and belong to space group P3221. A 2.9 Å native data set was collected at ESRF on beamline ID14‐2 with an Rmerge of 12.7%. Preliminary structural analysis provides a structural basis for the specific roles of DDAO.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>detergent</term></item><item><term>lipase</term></item><item><term>flap stabilization.</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2004-11">Published</change><change xml:id="refBibs-istex" who="#ISTEX-API" when="2016-1-4">References added</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/8DAD7EA4E8046AC3148EB40846CE1E985B53AC5E/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>Munksgaard International Publishers</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 Cryst. 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Mancheño, e‐mail: <email>xjosemi@iqfr.csic.es</email></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:AYD2.AYDts5035.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>Received 4 August 2004, accepted 27 September 2004</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">Crystallization of a proteolyzed form of the horse pancreatic lipase‐related protein 2: structural basis for the specific detergent requirement</title><title type="shortAuthors">Mancheño <i>et al.</i></title><title type="short">Horse pancreatic lipase‐related protein 2</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1"><personName><givenNames>José M.</givenNames><familyName>Mancheño</familyName></personName></creator><creator creatorRole="author" xml:id="cr2"><personName><givenNames>Sandrine</givenNames><familyName>Jayne</familyName></personName></creator><creator creatorRole="author" xml:id="cr3"><personName><givenNames>Brigritte</givenNames><familyName>Kerfelec</familyName></personName></creator><creator creatorRole="author" xml:id="cr4"><personName><givenNames>Catherine</givenNames><familyName>Chapus</familyName></personName></creator><creator creatorRole="author" xml:id="cr5"><personName><givenNames>Isabelle</givenNames><familyName>Crenon</familyName></personName></creator><creator creatorRole="author" xml:id="cr6"><personName><givenNames>Juan A.</givenNames><familyName>Hermoso</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="a1" countryCode="ES"><unparsedAffiliation>Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain</unparsedAffiliation></affiliation><affiliation xml:id="a2" countryCode="US"><unparsedAffiliation>INSERM‐U476 Nutrition Humaine et Lipides, 18 Avenue Mozart, 13009 Marseille, France</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en"><keyword xml:id="k1">detergent</keyword><keyword xml:id="k2">lipase</keyword><keyword xml:id="k3">flap stabilization.</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><p>Horse pancreatic lipase‐related proteins PLRP1 and PLRP2 are produced by the pancreas together with pancreatic lipase (PL). Sequence‐comparison analyses reveal that the three proteins possess the same two‐domain organization: an N‐terminal catalytic domain and a C‐terminal domain, which in PL is involved in colipase binding. Nevertheless, despite the high level of sequence identity found, they exhibit distinct enzymatic properties. The intrinsic sensitivity of the peptide bond between Ser245 and Thr246 within the flap region of PLRP2 to proteolytic cleavage probably complicates PLRP2 crystallization since, as shown here, this proteolyzed form of PLRP2 is only crystallized after specific detergent stabilization of this region. This has been performed by the hanging‐drop vapour‐diffusion method at 291 K and exclusively in the presence of <i>N</i>,<i>N</i>‐dimethyldecylamine‐β‐oxide (DDAO). However, most crystals (>95%) are highly twinned and diffract poorly (to ∼7–5 Å resolution). Diffraction‐quality trigonal crystals have unit‐cell parameters <i>a</i> = <i>b</i> = 128.4, <i>c</i> = 85.8 Å and belong to space group <i>P</i>3<sub>2</sub>21. A 2.9 Å native data set was collected at ESRF on beamline ID14‐2 with an <i>R</i><sub>merge</sub> of 12.7%. Preliminary structural analysis provides a structural basis for the specific roles of DDAO.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Crystallization of a proteolyzed form of the horse pancreatic lipase‐related protein 2: structural basis for the specific detergent requirement</title></titleInfo><titleInfo type="abbreviated"><title>Horse pancreatic lipase‐related protein 2</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Crystallization of a proteolyzed form of the horse pancreatic lipase‐related protein 2: structural basis for the specific detergent requirement</title></titleInfo><name type="personal"><namePart type="given">José M.</namePart><namePart type="family">Mancheño</namePart><affiliation>Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain</affiliation><affiliation>INSERM‐U476 Nutrition Humaine et Lipides, 18 Avenue Mozart, 13009 Marseille, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Sandrine</namePart><namePart type="family">Jayne</namePart><affiliation>Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain</affiliation><affiliation>INSERM‐U476 Nutrition Humaine et Lipides, 18 Avenue Mozart, 13009 Marseille, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Brigritte</namePart><namePart type="family">Kerfelec</namePart><affiliation>Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain</affiliation><affiliation>INSERM‐U476 Nutrition Humaine et Lipides, 18 Avenue Mozart, 13009 Marseille, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Catherine</namePart><namePart type="family">Chapus</namePart><affiliation>Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain</affiliation><affiliation>INSERM‐U476 Nutrition Humaine et Lipides, 18 Avenue Mozart, 13009 Marseille, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Isabelle</namePart><namePart type="family">Crenon</namePart><affiliation>Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain</affiliation><affiliation>INSERM‐U476 Nutrition Humaine et Lipides, 18 Avenue Mozart, 13009 Marseille, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Juan A.</namePart><namePart type="family">Hermoso</namePart><affiliation>Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain</affiliation><affiliation>INSERM‐U476 Nutrition Humaine et Lipides, 18 Avenue Mozart, 13009 Marseille, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article">article</genre><originInfo><publisher>Munksgaard International Publishers</publisher><place><placeTerm type="text">5 Abbey Square, Chester, Cheshire CH1 2HU, England</placeTerm></place><dateIssued encoding="w3cdtf">2004-11</dateIssued><edition>Received 4 August 2004, accepted 27 September 2004</edition><copyrightDate encoding="w3cdtf">2004</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">Horse pancreatic lipase‐related proteins PLRP1 and PLRP2 are produced by the pancreas together with pancreatic lipase (PL). Sequence‐comparison analyses reveal that the three proteins possess the same two‐domain organization: an N‐terminal catalytic domain and a C‐terminal domain, which in PL is involved in colipase binding. Nevertheless, despite the high level of sequence identity found, they exhibit distinct enzymatic properties. The intrinsic sensitivity of the peptide bond between Ser245 and Thr246 within the flap region of PLRP2 to proteolytic cleavage probably complicates PLRP2 crystallization since, as shown here, this proteolyzed form of PLRP2 is only crystallized after specific detergent stabilization of this region. This has been performed by the hanging‐drop vapour‐diffusion method at 291 K and exclusively in the presence of N,N‐dimethyldecylamine‐β‐oxide (DDAO). However, most crystals (>95%) are highly twinned and diffract poorly (to ∼7–5 Å resolution). Diffraction‐quality trigonal crystals have unit‐cell parameters a = b = 128.4, c = 85.8 Å and belong to space group P3221. A 2.9 Å native data set was collected at ESRF on beamline ID14‐2 with an Rmerge of 12.7%. Preliminary structural analysis provides a structural basis for the specific roles of DDAO.</abstract><subject lang="en"><genre>Keywords</genre><topic>detergent</topic><topic>lipase</topic><topic>flap stabilization.</topic></subject><relatedItem type="host"><titleInfo><title>Acta Crystallographica Section D</title></titleInfo><titleInfo type="abbreviated"><title>Acta Cryst. D</title></titleInfo><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>2004</date><detail type="volume"><caption>vol.</caption><number>60</number></detail><detail type="issue"><caption>no.</caption><number>11</number></detail><extent unit="pages"><start>2107</start><end>2109</end></extent></part></relatedItem><identifier type="istex">8DAD7EA4E8046AC3148EB40846CE1E985B53AC5E</identifier><identifier type="DOI">10.1107/S0907444904024229</identifier><identifier type="ArticleID">AYDTS5035</identifier><recordInfo><recordOrigin>Munksgaard International Publishers</recordOrigin><recordContentSource>WILEY</recordContentSource></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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