His22 of TLXI plays a critical role in the inhibition of glycoside hydrolase family 11 xylanases.
Identifieur interne : 000342 ( Main/Corpus ); précédent : 000341; suivant : 000343His22 of TLXI plays a critical role in the inhibition of glycoside hydrolase family 11 xylanases.
Auteurs : Sigrid Rombouts ; Ellen Fierens ; Elien Vandermarliere ; Arnout Voet ; Kurt Gebruers ; Johnny Beaugrand ; Christophe M. Courtin ; Jan A. Delcour ; Marc De Maeyer ; Anja Rabijns ; Steven Van Campenhout ; Guido VolckaertSource :
- Journal of enzyme inhibition and medicinal chemistry [ 1475-6374 ] ; 2009.
English descriptors
- KwdEn :
- Cloning, Molecular (MeSH), Endo-1,4-beta Xylanases (antagonists & inhibitors), Glycoside Hydrolases (antagonists & inhibitors), Histidine (MeSH), Models, Molecular (MeSH), Mutagenesis, Site-Directed (MeSH), Plant Proteins (genetics), Plant Proteins (physiology), Protein Binding (MeSH), Triticum (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Endo-1,4-beta Xylanases, Glycoside Hydrolases.
- chemical , genetics : Plant Proteins.
- chemical , physiology : Plant Proteins.
- Cloning, Molecular, Histidine, Models, Molecular, Mutagenesis, Site-Directed, Protein Binding, Triticum.
Abstract
Recently, a novel wheat thaumatin-like protein, TLXI, which inhibits microbial glycoside hydrolase family (GH) 11 xylanases has been identified. It is the first xylanase inhibitor that exerts its inhibition in a non-competitive way. In the present study we gained insight into the interaction between TLXI and xylanases via combined molecular modeling and mutagenic approaches. More specifically, site-specific mutation of His22, situated on a loop which distinguishes TLXI from other, non-inhibiting, thaumatin-like proteins, and subsequent expression of the mutant in Pichia pastoris resulted in a protein lacking inhibition capacity. The mutant protein was unable to form a complex with GH11 xylanases. Based on these findings, the interaction of TLXI with GH11 xylanases is discussed.
DOI: 10.1080/14756360701841913
PubMed: 18608747
Links to Exploration step
pubmed:18608747Le document en format XML
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Courtin</name></author><author><name sortKey="Delcour, Jan A" sort="Delcour, Jan A" uniqKey="Delcour J" first="Jan A" last="Delcour">Jan A. Delcour</name></author><author><name sortKey="De Maeyer, Marc" sort="De Maeyer, Marc" uniqKey="De Maeyer M" first="Marc" last="De Maeyer">Marc De Maeyer</name></author><author><name sortKey="Rabijns, Anja" sort="Rabijns, Anja" uniqKey="Rabijns A" first="Anja" last="Rabijns">Anja Rabijns</name></author><author><name sortKey="Van Campenhout, Steven" sort="Van Campenhout, Steven" uniqKey="Van Campenhout S" first="Steven" last="Van Campenhout">Steven Van Campenhout</name></author><author><name sortKey="Volckaert, Guido" sort="Volckaert, Guido" uniqKey="Volckaert G" first="Guido" last="Volckaert">Guido Volckaert</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:18608747</idno><idno type="pmid">18608747</idno><idno type="doi">10.1080/14756360701841913</idno><idno type="wicri:Area/Main/Corpus">000342</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000342</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">His22 of TLXI plays a critical role in the inhibition of glycoside hydrolase family 11 xylanases.</title><author><name sortKey="Rombouts, Sigrid" sort="Rombouts, Sigrid" uniqKey="Rombouts S" first="Sigrid" last="Rombouts">Sigrid Rombouts</name><affiliation><nlm:affiliation>Laboratory of Gene Technology, Katholieke Universiteit Leuven, Leuven, Belgium.</nlm:affiliation></affiliation></author><author><name sortKey="Fierens, Ellen" sort="Fierens, Ellen" uniqKey="Fierens E" first="Ellen" last="Fierens">Ellen Fierens</name></author><author><name sortKey="Vandermarliere, Elien" sort="Vandermarliere, Elien" uniqKey="Vandermarliere E" first="Elien" last="Vandermarliere">Elien Vandermarliere</name></author><author><name sortKey="Voet, Arnout" sort="Voet, Arnout" uniqKey="Voet A" first="Arnout" last="Voet">Arnout Voet</name></author><author><name sortKey="Gebruers, Kurt" sort="Gebruers, Kurt" uniqKey="Gebruers K" first="Kurt" last="Gebruers">Kurt Gebruers</name></author><author><name sortKey="Beaugrand, Johnny" sort="Beaugrand, Johnny" uniqKey="Beaugrand J" first="Johnny" last="Beaugrand">Johnny Beaugrand</name></author><author><name sortKey="Courtin, Christophe M" sort="Courtin, Christophe M" uniqKey="Courtin C" first="Christophe M" last="Courtin">Christophe M. Courtin</name></author><author><name sortKey="Delcour, Jan A" sort="Delcour, Jan A" uniqKey="Delcour J" first="Jan A" last="Delcour">Jan A. Delcour</name></author><author><name sortKey="De Maeyer, Marc" sort="De Maeyer, Marc" uniqKey="De Maeyer M" first="Marc" last="De Maeyer">Marc De Maeyer</name></author><author><name sortKey="Rabijns, Anja" sort="Rabijns, Anja" uniqKey="Rabijns A" first="Anja" last="Rabijns">Anja Rabijns</name></author><author><name sortKey="Van Campenhout, Steven" sort="Van Campenhout, Steven" uniqKey="Van Campenhout S" first="Steven" last="Van Campenhout">Steven Van Campenhout</name></author><author><name sortKey="Volckaert, Guido" sort="Volckaert, Guido" uniqKey="Volckaert G" first="Guido" last="Volckaert">Guido Volckaert</name></author></analytic><series><title level="j">Journal of enzyme inhibition and medicinal chemistry</title><idno type="eISSN">1475-6374</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cloning, Molecular (MeSH)</term><term>Endo-1,4-beta Xylanases (antagonists & inhibitors)</term><term>Glycoside Hydrolases (antagonists & inhibitors)</term><term>Histidine (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Plant Proteins (genetics)</term><term>Plant Proteins (physiology)</term><term>Protein Binding (MeSH)</term><term>Triticum (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Endo-1,4-beta Xylanases</term><term>Glycoside Hydrolases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cloning, Molecular</term><term>Histidine</term><term>Models, Molecular</term><term>Mutagenesis, Site-Directed</term><term>Protein Binding</term><term>Triticum</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Recently, a novel wheat thaumatin-like protein, TLXI, which inhibits microbial glycoside hydrolase family (GH) 11 xylanases has been identified. It is the first xylanase inhibitor that exerts its inhibition in a non-competitive way. In the present study we gained insight into the interaction between TLXI and xylanases via combined molecular modeling and mutagenic approaches. More specifically, site-specific mutation of His22, situated on a loop which distinguishes TLXI from other, non-inhibiting, thaumatin-like proteins, and subsequent expression of the mutant in Pichia pastoris resulted in a protein lacking inhibition capacity. The mutant protein was unable to form a complex with GH11 xylanases. Based on these findings, the interaction of TLXI with GH11 xylanases is discussed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18608747</PMID><DateCompleted><Year>2009</Year><Month>03</Month><Day>23</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>16</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1475-6374</ISSN><JournalIssue CitedMedium="Internet"><Volume>24</Volume><Issue>1</Issue><PubDate><Year>2009</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Journal of enzyme inhibition and medicinal chemistry</Title><ISOAbbreviation>J Enzyme Inhib Med Chem</ISOAbbreviation></Journal><ArticleTitle>His22 of TLXI plays a critical role in the inhibition of glycoside hydrolase family 11 xylanases.</ArticleTitle><Pagination><MedlinePgn>38-46</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1080/14756360701841913 </ELocationID><Abstract><AbstractText>Recently, a novel wheat thaumatin-like protein, TLXI, which inhibits microbial glycoside hydrolase family (GH) 11 xylanases has been identified. It is the first xylanase inhibitor that exerts its inhibition in a non-competitive way. In the present study we gained insight into the interaction between TLXI and xylanases via combined molecular modeling and mutagenic approaches. More specifically, site-specific mutation of His22, situated on a loop which distinguishes TLXI from other, non-inhibiting, thaumatin-like proteins, and subsequent expression of the mutant in Pichia pastoris resulted in a protein lacking inhibition capacity. The mutant protein was unable to form a complex with GH11 xylanases. Based on these findings, the interaction of TLXI with GH11 xylanases is discussed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rombouts</LastName><ForeName>Sigrid</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Laboratory of Gene Technology, Katholieke Universiteit Leuven, Leuven, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fierens</LastName><ForeName>Ellen</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Vandermarliere</LastName><ForeName>Elien</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Voet</LastName><ForeName>Arnout</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Gebruers</LastName><ForeName>Kurt</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Beaugrand</LastName><ForeName>Johnny</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Courtin</LastName><ForeName>Christophe M</ForeName><Initials>CM</Initials></Author><Author ValidYN="Y"><LastName>Delcour</LastName><ForeName>Jan A</ForeName><Initials>JA</Initials></Author><Author ValidYN="Y"><LastName>de Maeyer</LastName><ForeName>Marc</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Rabijns</LastName><ForeName>Anja</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Van Campenhout</LastName><ForeName>Steven</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Volckaert</LastName><ForeName>Guido</ForeName><Initials>G</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></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Enzyme Inhib Med Chem</MedlineTA><NlmUniqueID>101150203</NlmUniqueID><ISSNLinking>1475-6366</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>4QD397987E</RegistryNumber><NameOfSubstance UI="D006639">Histidine</NameOfSubstance></Chemical><Chemical><RegistryNumber>53850-34-3</RegistryNumber><NameOfSubstance UI="C003427">thaumatin protein, plant</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="D006026">Glycoside Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.8</RegistryNumber><NameOfSubstance UI="D043364">Endo-1,4-beta Xylanases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D043364" MajorTopicYN="N">Endo-1,4-beta Xylanases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006026" MajorTopicYN="N">Glycoside Hydrolases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006639" MajorTopicYN="Y">Histidine</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014908" MajorTopicYN="N">Triticum</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>7</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>3</Month><Day>24</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>7</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18608747</ArticleId><ArticleId IdType="pii">793963090</ArticleId><ArticleId IdType="doi">10.1080/14756360701841913</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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