Family 7 cellobiohydrolases from Phanerochaete chrysosporium: crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 A resolution and homology models of the isozymes.
Identifieur interne : 000A43 ( Main/Exploration ); précédent : 000A42; suivant : 000A44Family 7 cellobiohydrolases from Phanerochaete chrysosporium: crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 A resolution and homology models of the isozymes.
Auteurs : I G Mu Oz [Suède] ; W. Ubhayasekera ; H. Henriksson ; I. Szab ; G. Pettersson ; G. Johansson ; S L Mowbray ; J. St HlbergSource :
- Journal of molecular biology [ 0022-2836 ] ; 2001.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Cellulase (classification), Cellulase (composition chimique), Cellulose 1,4-beta-cellobiosidase (MeSH), Cristallographie aux rayons X (MeSH), Domaine catalytique (MeSH), Données de séquences moléculaires (MeSH), Isoenzymes (classification), Isoenzymes (composition chimique), Liaison hydrogène (MeSH), Modèles moléculaires (MeSH), Phanerochaete (enzymologie), Similitude de séquences d'acides aminés (MeSH), Sites de fixation (MeSH), Structure secondaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Trichoderma (enzymologie).
- MESH :
- classification : Cellulase, Isoenzymes.
- composition chimique : Cellulase, Isoenzymes.
- enzymologie : Phanerochaete, Trichoderma.
- Alignement de séquences, Cellulose 1,4-beta-cellobiosidase, Cristallographie aux rayons X, Domaine catalytique, Données de séquences moléculaires, Liaison hydrogène, Modèles moléculaires, Similitude de séquences d'acides aminés, Sites de fixation, Structure secondaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Binding Sites (MeSH), Catalytic Domain (MeSH), Cellulase (chemistry), Cellulase (classification), Cellulose 1,4-beta-Cellobiosidase (MeSH), Crystallography, X-Ray (MeSH), Hydrogen Bonding (MeSH), Isoenzymes (chemistry), Isoenzymes (classification), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Phanerochaete (enzymology), Protein Structure, Secondary (MeSH), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Trichoderma (enzymology).
- MESH :
- chemical , chemistry : Cellulase, Isoenzymes.
- chemical , classification : Cellulase, Isoenzymes.
- enzymology : Phanerochaete, Trichoderma.
- Amino Acid Sequence, Binding Sites, Catalytic Domain, Cellulose 1,4-beta-Cellobiosidase, Crystallography, X-Ray, Hydrogen Bonding, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Sequence Alignment, Sequence Homology, Amino Acid.
Abstract
Cellobiohydrolase 58 (Cel7D) is the major cellulase produced by the white-rot fungus Phanerochaete chrysosporium, constituting approximately 10 % of the total secreted protein in liquid culture on cellulose. The enzyme is classified into family 7 of the glycosyl hydrolases, together with cellobiohydrolase I (Cel7A) and endoglucanase I (Cel7B) from Trichoderma reesei. Like those enzymes, it catalyses cellulose hydrolysis with net retention of the anomeric carbon configuration. The structure of the catalytic module (431 residues) of Cel7D was determined at 3.0 A resolution using the structure of Cel7A from T. reesei as a search model in molecular replacement, and ultimately refined at 1.32 A resolution. The core structure is a beta-sandwich composed of two large and mainly antiparallel beta-sheets packed onto each other. A long cellulose-binding groove is formed by loops on one face of the sandwich. The catalytic residues are conserved and the mechanism is expected to be the same as for other family members. The Phanerochaete Cel7D binding site is more open than that of the T. reesei cellobiohydrolase, as a result of deletions and other changes in the loop regions, which may explain observed differences in catalytic properties. The binding site is not, however, as open as the groove of the corresponding endoglucanase. A tyrosine residue at the entrance of the tunnel may be part of an additional subsite not present in the T. reesei cellobiohydrolase. The Cel7D structure was used to model the products of the five other family 7 genes found in P. chrysosporium. The results suggest that at least two of these will have differences in specificity and possibly catalytic mechanism, thus offering some explanation for the presence of Cel7 isozymes in this species, which are differentially expressed in response to various growth conditions.
DOI: 10.1006/jmbi.2000.5180
PubMed: 11743726
Affiliations:
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Ubhayasekera</name></author><author><name sortKey="Henriksson, H" sort="Henriksson, H" uniqKey="Henriksson H" first="H" last="Henriksson">H. Henriksson</name></author><author><name sortKey="Szab, I" sort="Szab, I" uniqKey="Szab I" first="I" last="Szab">I. Szab</name></author><author><name sortKey="Pettersson, G" sort="Pettersson, G" uniqKey="Pettersson G" first="G" last="Pettersson">G. Pettersson</name></author><author><name sortKey="Johansson, G" sort="Johansson, G" uniqKey="Johansson G" first="G" last="Johansson">G. Johansson</name></author><author><name sortKey="Mowbray, S L" sort="Mowbray, S L" uniqKey="Mowbray S" first="S L" last="Mowbray">S L Mowbray</name></author><author><name sortKey="St Hlberg, J" sort="St Hlberg, J" uniqKey="St Hlberg J" first="J" last="St Hlberg">J. St Hlberg</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2001">2001</date><idno type="RBID">pubmed:11743726</idno><idno type="pmid">11743726</idno><idno type="doi">10.1006/jmbi.2000.5180</idno><idno type="wicri:Area/Main/Corpus">000A27</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000A27</idno><idno type="wicri:Area/Main/Curation">000A27</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000A27</idno><idno type="wicri:Area/Main/Exploration">000A27</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Family 7 cellobiohydrolases from Phanerochaete chrysosporium: crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 A resolution and homology models of the isozymes.</title><author><name sortKey="Mu Oz, I G" sort="Mu Oz, I G" uniqKey="Mu Oz I" first="I G" last="Mu Oz">I G Mu Oz</name><affiliation wicri:level="1"><nlm:affiliation>Department of Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Centre, SE-751 24 Uppsala, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Centre, SE-751 24 Uppsala</wicri:regionArea><wicri:noRegion>SE-751 24 Uppsala</wicri:noRegion></affiliation></author><author><name sortKey="Ubhayasekera, W" sort="Ubhayasekera, W" uniqKey="Ubhayasekera W" first="W" last="Ubhayasekera">W. Ubhayasekera</name></author><author><name sortKey="Henriksson, H" sort="Henriksson, H" uniqKey="Henriksson H" first="H" last="Henriksson">H. Henriksson</name></author><author><name sortKey="Szab, I" sort="Szab, I" uniqKey="Szab I" first="I" last="Szab">I. Szab</name></author><author><name sortKey="Pettersson, G" sort="Pettersson, G" uniqKey="Pettersson G" first="G" last="Pettersson">G. Pettersson</name></author><author><name sortKey="Johansson, G" sort="Johansson, G" uniqKey="Johansson G" first="G" last="Johansson">G. Johansson</name></author><author><name sortKey="Mowbray, S L" sort="Mowbray, S L" uniqKey="Mowbray S" first="S L" last="Mowbray">S L Mowbray</name></author><author><name sortKey="St Hlberg, J" sort="St Hlberg, J" uniqKey="St Hlberg J" first="J" last="St Hlberg">J. St Hlberg</name></author></analytic><series><title level="j">Journal of molecular biology</title><idno type="ISSN">0022-2836</idno><imprint><date when="2001" type="published">2001</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>Catalytic Domain (MeSH)</term><term>Cellulase (chemistry)</term><term>Cellulase (classification)</term><term>Cellulose 1,4-beta-Cellobiosidase (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Hydrogen Bonding (MeSH)</term><term>Isoenzymes (chemistry)</term><term>Isoenzymes (classification)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Phanerochaete (enzymology)</term><term>Protein Structure, Secondary (MeSH)</term><term>Sequence Alignment (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Trichoderma (enzymology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Cellulase (classification)</term><term>Cellulase (composition chimique)</term><term>Cellulose 1,4-beta-cellobiosidase (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Domaine catalytique (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Isoenzymes (classification)</term><term>Isoenzymes (composition chimique)</term><term>Liaison hydrogène (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Phanerochaete (enzymologie)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Sites de fixation (MeSH)</term><term>Structure secondaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Trichoderma (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cellulase</term><term>Isoenzymes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="classification" xml:lang="en"><term>Cellulase</term><term>Isoenzymes</term></keywords><keywords scheme="MESH" qualifier="classification" xml:lang="fr"><term>Cellulase</term><term>Isoenzymes</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cellulase</term><term>Isoenzymes</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term><term>Trichoderma</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term><term>Trichoderma</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Catalytic Domain</term><term>Cellulose 1,4-beta-Cellobiosidase</term><term>Crystallography, X-Ray</term><term>Hydrogen Bonding</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Structure, Secondary</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Cellulose 1,4-beta-cellobiosidase</term><term>Cristallographie aux rayons X</term><term>Domaine catalytique</term><term>Données de séquences moléculaires</term><term>Liaison hydrogène</term><term>Modèles moléculaires</term><term>Similitude de séquences d'acides aminés</term><term>Sites de fixation</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cellobiohydrolase 58 (Cel7D) is the major cellulase produced by the white-rot fungus Phanerochaete chrysosporium, constituting approximately 10 % of the total secreted protein in liquid culture on cellulose. The enzyme is classified into family 7 of the glycosyl hydrolases, together with cellobiohydrolase I (Cel7A) and endoglucanase I (Cel7B) from Trichoderma reesei. Like those enzymes, it catalyses cellulose hydrolysis with net retention of the anomeric carbon configuration. The structure of the catalytic module (431 residues) of Cel7D was determined at 3.0 A resolution using the structure of Cel7A from T. reesei as a search model in molecular replacement, and ultimately refined at 1.32 A resolution. The core structure is a beta-sandwich composed of two large and mainly antiparallel beta-sheets packed onto each other. A long cellulose-binding groove is formed by loops on one face of the sandwich. The catalytic residues are conserved and the mechanism is expected to be the same as for other family members. The Phanerochaete Cel7D binding site is more open than that of the T. reesei cellobiohydrolase, as a result of deletions and other changes in the loop regions, which may explain observed differences in catalytic properties. The binding site is not, however, as open as the groove of the corresponding endoglucanase. A tyrosine residue at the entrance of the tunnel may be part of an additional subsite not present in the T. reesei cellobiohydrolase. The Cel7D structure was used to model the products of the five other family 7 genes found in P. chrysosporium. The results suggest that at least two of these will have differences in specificity and possibly catalytic mechanism, thus offering some explanation for the presence of Cel7 isozymes in this species, which are differentially expressed in response to various growth conditions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11743726</PMID><DateCompleted><Year>2002</Year><Month>02</Month><Day>06</Day></DateCompleted><DateRevised><Year>2009</Year><Month>11</Month><Day>03</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-2836</ISSN><JournalIssue CitedMedium="Print"><Volume>314</Volume><Issue>5</Issue><PubDate><Year>2001</Year><Month>Dec</Month><Day>14</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J Mol Biol</ISOAbbreviation></Journal><ArticleTitle>Family 7 cellobiohydrolases from Phanerochaete chrysosporium: crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 A resolution and homology models of the isozymes.</ArticleTitle><Pagination><MedlinePgn>1097-111</MedlinePgn></Pagination><Abstract><AbstractText>Cellobiohydrolase 58 (Cel7D) is the major cellulase produced by the white-rot fungus Phanerochaete chrysosporium, constituting approximately 10 % of the total secreted protein in liquid culture on cellulose. The enzyme is classified into family 7 of the glycosyl hydrolases, together with cellobiohydrolase I (Cel7A) and endoglucanase I (Cel7B) from Trichoderma reesei. Like those enzymes, it catalyses cellulose hydrolysis with net retention of the anomeric carbon configuration. The structure of the catalytic module (431 residues) of Cel7D was determined at 3.0 A resolution using the structure of Cel7A from T. reesei as a search model in molecular replacement, and ultimately refined at 1.32 A resolution. The core structure is a beta-sandwich composed of two large and mainly antiparallel beta-sheets packed onto each other. A long cellulose-binding groove is formed by loops on one face of the sandwich. The catalytic residues are conserved and the mechanism is expected to be the same as for other family members. The Phanerochaete Cel7D binding site is more open than that of the T. reesei cellobiohydrolase, as a result of deletions and other changes in the loop regions, which may explain observed differences in catalytic properties. The binding site is not, however, as open as the groove of the corresponding endoglucanase. A tyrosine residue at the entrance of the tunnel may be part of an additional subsite not present in the T. reesei cellobiohydrolase. The Cel7D structure was used to model the products of the five other family 7 genes found in P. chrysosporium. The results suggest that at least two of these will have differences in specificity and possibly catalytic mechanism, thus offering some explanation for the presence of Cel7 isozymes in this species, which are differentially expressed in response to various growth conditions.</AbstractText><CopyrightInformation>Copyright 2001 Academic Press.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Muñoz</LastName><ForeName>I G</ForeName><Initials>IG</Initials><AffiliationInfo><Affiliation>Department of Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Centre, SE-751 24 Uppsala, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ubhayasekera</LastName><ForeName>W</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Henriksson</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Szabó</LastName><ForeName>I</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Pettersson</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Johansson</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Mowbray</LastName><ForeName>S L</ForeName><Initials>SL</Initials></Author><Author ValidYN="Y"><LastName>Ståhlberg</LastName><ForeName>J</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><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 Mol Biol</MedlineTA><NlmUniqueID>2985088R</NlmUniqueID><ISSNLinking>0022-2836</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.4</RegistryNumber><NameOfSubstance UI="D002480">Cellulase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.91</RegistryNumber><NameOfSubstance UI="D043366">Cellulose 1,4-beta-Cellobiosidase</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="D020134" MajorTopicYN="Y">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002480" MajorTopicYN="N">Cellulase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000145" MajorTopicYN="Y">classification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D043366" MajorTopicYN="N">Cellulose 1,4-beta-Cellobiosidase</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006860" MajorTopicYN="N">Hydrogen Bonding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="Y">Models, Molecular</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="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="Y">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014242" MajorTopicYN="N">Trichoderma</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year><Month>12</Month><Day>18</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>2</Month><Day>7</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2001</Year><Month>12</Month><Day>18</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11743726</ArticleId><ArticleId IdType="doi">10.1006/jmbi.2000.5180</ArticleId><ArticleId IdType="pii">S0022-2836(00)95180-5</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country></list><tree><noCountry><name sortKey="Henriksson, H" sort="Henriksson, H" uniqKey="Henriksson H" first="H" last="Henriksson">H. Henriksson</name><name sortKey="Johansson, G" sort="Johansson, G" uniqKey="Johansson G" first="G" last="Johansson">G. Johansson</name><name sortKey="Mowbray, S L" sort="Mowbray, S L" uniqKey="Mowbray S" first="S L" last="Mowbray">S L Mowbray</name><name sortKey="Pettersson, G" sort="Pettersson, G" uniqKey="Pettersson G" first="G" last="Pettersson">G. Pettersson</name><name sortKey="St Hlberg, J" sort="St Hlberg, J" uniqKey="St Hlberg J" first="J" last="St Hlberg">J. St Hlberg</name><name sortKey="Szab, I" sort="Szab, I" uniqKey="Szab I" first="I" last="Szab">I. Szab</name><name sortKey="Ubhayasekera, W" sort="Ubhayasekera, W" uniqKey="Ubhayasekera W" first="W" last="Ubhayasekera">W. Ubhayasekera</name></noCountry><country name="Suède"><noRegion><name sortKey="Mu Oz, I G" sort="Mu Oz, I G" uniqKey="Mu Oz I" first="I G" last="Mu Oz">I G Mu Oz</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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