Crystal structure of intracellular family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium.
Identifieur interne : 000736 ( Main/Exploration ); précédent : 000735; suivant : 000737Crystal structure of intracellular family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium.
Auteurs : Yuri Nijikken [Japon] ; Takeshi Tsukada ; Kiyohiko Igarashi ; Masahiro Samejima ; Takayoshi Wakagi ; Hirofumi Shoun ; Shinya FushinobuSource :
- FEBS letters [ 0014-5793 ] ; 2007.
Descripteurs français
- KwdFr :
- Chromatographie sur gel (MeSH), Conformation des protéines (MeSH), Cristallographie aux rayons X (MeSH), Données de séquences moléculaires (MeSH), Gluconates (composition chimique), Lactones (MeSH), Phanerochaete (enzymologie), Protéines fongiques (composition chimique), Sites de fixation (MeSH), Séquence d'acides aminés (MeSH), bêta-Glucosidase (composition chimique).
- MESH :
- composition chimique : Gluconates, Protéines fongiques, bêta-Glucosidase.
- enzymologie : Phanerochaete.
- Chromatographie sur gel, Conformation des protéines, Cristallographie aux rayons X, Données de séquences moléculaires, Lactones, Sites de fixation, Séquence d'acides aminés.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Fungal Proteins, Gluconates, beta-Glucosidase.
- enzymology : Phanerochaete.
- Amino Acid Sequence, Binding Sites, Chromatography, Gel, Crystallography, X-Ray, Lactones, Molecular Sequence Data, Protein Conformation.
Abstract
The white-rot fungus Phanerochaete chrysosporium has two intracellular beta-glucosidases (BGL1A and BGL1B) belonging to glycoside hydrolase (GH) family 1. BGL1B effectively hydrolyzes cellobiose and cellobionolactone, but BGL1A does not. We have determined the crystal structure of BGL1A in substrate-free and gluconolactone complexed forms. The overall structure and the characteristic of subsite -1 (glycone site) were similar to those of other known GH1 enzymes. The loop regions covering on the (beta/alpha)(8) barrel was significantly deviated, and they form a unique subsite +1 (aglycone site) of BGL1A.
DOI: 10.1016/j.febslet.2007.03.009
PubMed: 17376440
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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sortKey="Shoun, Hirofumi" sort="Shoun, Hirofumi" uniqKey="Shoun H" first="Hirofumi" last="Shoun">Hirofumi Shoun</name></author><author><name sortKey="Fushinobu, Shinya" sort="Fushinobu, Shinya" uniqKey="Fushinobu S" first="Shinya" last="Fushinobu">Shinya Fushinobu</name></author></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Binding Sites (MeSH)</term><term>Chromatography, Gel (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Fungal Proteins (chemistry)</term><term>Gluconates (chemistry)</term><term>Lactones (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Phanerochaete (enzymology)</term><term>Protein Conformation (MeSH)</term><term>beta-Glucosidase (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chromatographie sur gel (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Gluconates (composition chimique)</term><term>Lactones (MeSH)</term><term>Phanerochaete (enzymologie)</term><term>Protéines fongiques (composition chimique)</term><term>Sites de fixation (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>bêta-Glucosidase (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fungal Proteins</term><term>Gluconates</term><term>beta-Glucosidase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Gluconates</term><term>Protéines fongiques</term><term>bêta-Glucosidase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Chromatography, Gel</term><term>Crystallography, X-Ray</term><term>Lactones</term><term>Molecular Sequence Data</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie sur gel</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Lactones</term><term>Sites de fixation</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The white-rot fungus Phanerochaete chrysosporium has two intracellular beta-glucosidases (BGL1A and BGL1B) belonging to glycoside hydrolase (GH) family 1. BGL1B effectively hydrolyzes cellobiose and cellobionolactone, but BGL1A does not. We have determined the crystal structure of BGL1A in substrate-free and gluconolactone complexed forms. The overall structure and the characteristic of subsite -1 (glycone site) were similar to those of other known GH1 enzymes. The loop regions covering on the (beta/alpha)(8) barrel was significantly deviated, and they form a unique subsite +1 (aglycone site) of BGL1A.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17376440</PMID><DateCompleted><Year>2007</Year><Month>06</Month><Day>06</Day></DateCompleted><DateRevised><Year>2012</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>581</Volume><Issue>7</Issue><PubDate><Year>2007</Year><Month>Apr</Month><Day>03</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Crystal structure of intracellular family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>1514-20</MedlinePgn></Pagination><Abstract><AbstractText>The white-rot fungus Phanerochaete chrysosporium has two intracellular beta-glucosidases (BGL1A and BGL1B) belonging to glycoside hydrolase (GH) family 1. BGL1B effectively hydrolyzes cellobiose and cellobionolactone, but BGL1A does not. We have determined the crystal structure of BGL1A in substrate-free and gluconolactone complexed forms. The overall structure and the characteristic of subsite -1 (glycone site) were similar to those of other known GH1 enzymes. The loop regions covering on the (beta/alpha)(8) barrel was significantly deviated, and they form a unique subsite +1 (aglycone site) of BGL1A.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nijikken</LastName><ForeName>Yuri</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, The University of Tokyo, 1-1-1 Yayoi, Tokyo 113-8657, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tsukada</LastName><ForeName>Takeshi</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Igarashi</LastName><ForeName>Kiyohiko</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Samejima</LastName><ForeName>Masahiro</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Wakagi</LastName><ForeName>Takayoshi</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Shoun</LastName><ForeName>Hirofumi</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Fushinobu</LastName><ForeName>Shinya</ForeName><Initials>S</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><ArticleDate DateType="Electronic"><Year>2007</Year><Month>03</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005942">Gluconates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007783">Lactones</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.21</RegistryNumber><NameOfSubstance UI="D001617">beta-Glucosidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>WQ29KQ9POT</RegistryNumber><NameOfSubstance UI="C010730">beta-glucono-1,5-lactone</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002850" MajorTopicYN="N">Chromatography, Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005942" MajorTopicYN="N">Gluconates</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007783" MajorTopicYN="N">Lactones</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001617" MajorTopicYN="N">beta-Glucosidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>12</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2007</Year><Month>03</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2007</Year><Month>03</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>3</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>6</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>3</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17376440</ArticleId><ArticleId IdType="pii">S0014-5793(07)00259-1</ArticleId><ArticleId IdType="doi">10.1016/j.febslet.2007.03.009</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement><orgName><li>Université de Tokyo</li></orgName></list><tree><noCountry><name sortKey="Fushinobu, Shinya" sort="Fushinobu, Shinya" uniqKey="Fushinobu S" first="Shinya" last="Fushinobu">Shinya Fushinobu</name><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name><name sortKey="Shoun, Hirofumi" sort="Shoun, Hirofumi" uniqKey="Shoun H" first="Hirofumi" last="Shoun">Hirofumi Shoun</name><name sortKey="Tsukada, Takeshi" sort="Tsukada, Takeshi" uniqKey="Tsukada T" first="Takeshi" last="Tsukada">Takeshi Tsukada</name><name sortKey="Wakagi, Takayoshi" sort="Wakagi, Takayoshi" uniqKey="Wakagi T" first="Takayoshi" last="Wakagi">Takayoshi Wakagi</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Nijikken, Yuri" sort="Nijikken, Yuri" uniqKey="Nijikken Y" first="Yuri" last="Nijikken">Yuri Nijikken</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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