WhiteRotV1, Main, Exploration, bibRecord, 000594

Crystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium.

Identifieur interne : 000594 ( Main/Exploration ); précédent : 000593; suivant : 000595

Crystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium.

Auteurs : Mikako Tachioka [Japon] ; Akihiko Nakamura [Japon] ; Takuya Ishida [Japon] ; Kiyohiko Igarashi [Japon] ; Masahiro Samejima [Japon]

Source :

Acta crystallographica. Section F, Structural biology communications [ 2053-230X ] ; 2017.

RBID : pubmed:28695848

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Motifs (MeSH), Catalytic Domain (MeSH), Cellulose 1,4-beta-Cellobiosidase (chemistry), Cellulose 1,4-beta-Cellobiosidase (genetics), Cellulose 1,4-beta-Cellobiosidase (metabolism), Cloning, Molecular (MeSH), Crystallography, X-Ray (MeSH), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression (MeSH), Hydrophobic and Hydrophilic Interactions (MeSH), Models, Molecular (MeSH), Nitrobenzenes (chemistry), Phanerochaete (chemistry), Phanerochaete (enzymology), Pichia (genetics), Pichia (metabolism), Protein Binding (MeSH), Protein Conformation, alpha-Helical (MeSH), Protein Conformation, beta-Strand (MeSH), Protein Interaction Domains and Motifs (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Substrate Specificity (MeSH), Trisaccharides (chemistry).
MESH :
- chemical , chemistry : Cellulose 1,4-beta-Cellobiosidase, Fungal Proteins, Nitrobenzenes, Recombinant Proteins, Trisaccharides.
- chemical , genetics : Cellulose 1,4-beta-Cellobiosidase, Fungal Proteins, Recombinant Proteins.
- chemical , metabolism : Cellulose 1,4-beta-Cellobiosidase, Fungal Proteins, Recombinant Proteins.
- chemistry : Phanerochaete.
- enzymology : Phanerochaete.
- genetics : Pichia.
- metabolism : Pichia.
- Amino Acid Motifs, Catalytic Domain, Cloning, Molecular, Crystallography, X-Ray, Gene Expression, Hydrophobic and Hydrophilic Interactions, Models, Molecular, Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Substrate Specificity.

Abstract

Cellobiohydrolases belonging to glycoside hydrolase family 6 (CBH II, Cel6A) play key roles in the hydrolysis of crystalline cellulose. CBH II from the white-rot fungus Phanerochaete chrysosporium (PcCel6A) consists of a catalytic domain (CD) and a carbohydrate-binding module connected by a linker peptide, like other known fungal cellobiohydrolases. In the present study, the CD of PcCel6A was crystallized without ligands, and p-nitrophenyl β-D-cellotrioside (pNPG3) was soaked into the crystals. The determined structures of the ligand-free and pNPG3-soaked crystals revealed that binding of cellobiose at substrate subsites +1 and +2 induces a conformational change of the N-terminal and C-terminal loops, switching the tunnel-shaped active site from the open to the closed form.

DOI: 10.1107/S2053230X17008093
PubMed: 28695848
PubMed Central: PMC5505244

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000538
to stream Main, to step Curation: 000538

Le document en format XML

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<author><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (MeSH)</term>
<term>Catalytic Domain (MeSH)</term>
<term>Cellulose 1,4-beta-Cellobiosidase (chemistry)</term>
<term>Cellulose 1,4-beta-Cellobiosidase (genetics)</term>
<term>Cellulose 1,4-beta-Cellobiosidase (metabolism)</term>
<term>Cloning, Molecular (MeSH)</term>
<term>Crystallography, X-Ray (MeSH)</term>
<term>Fungal Proteins (chemistry)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Gene Expression (MeSH)</term>
<term>Hydrophobic and Hydrophilic Interactions (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Nitrobenzenes (chemistry)</term>
<term>Phanerochaete (chemistry)</term>
<term>Phanerochaete (enzymology)</term>
<term>Pichia (genetics)</term>
<term>Pichia (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Conformation, alpha-Helical (MeSH)</term>
<term>Protein Conformation, beta-Strand (MeSH)</term>
<term>Protein Interaction Domains and Motifs (MeSH)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Substrate Specificity (MeSH)</term>
<term>Trisaccharides (chemistry)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Cellulose 1,4-beta-cellobiosidase (composition chimique)</term>
<term>Cellulose 1,4-beta-cellobiosidase (génétique)</term>
<term>Cellulose 1,4-beta-cellobiosidase (métabolisme)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Cristallographie aux rayons X (MeSH)</term>
<term>Domaine catalytique (MeSH)</term>
<term>Expression des gènes (MeSH)</term>
<term>Interactions hydrophobes et hydrophiles (MeSH)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Motifs d'acides aminés (MeSH)</term>
<term>Motifs et domaines d'intéraction protéique (MeSH)</term>
<term>Nitrobenzènes (composition chimique)</term>
<term>Phanerochaete (composition chimique)</term>
<term>Phanerochaete (enzymologie)</term>
<term>Pichia (génétique)</term>
<term>Pichia (métabolisme)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Protéines fongiques (génétique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Protéines recombinantes (composition chimique)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Spécificité du substrat (MeSH)</term>
<term>Structure en brin bêta (MeSH)</term>
<term>Structure en hélice alpha (MeSH)</term>
<term>Triholosides (composition chimique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cellulose 1,4-beta-Cellobiosidase</term>
<term>Fungal Proteins</term>
<term>Nitrobenzenes</term>
<term>Recombinant Proteins</term>
<term>Trisaccharides</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cellulose 1,4-beta-Cellobiosidase</term>
<term>Fungal Proteins</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cellulose 1,4-beta-Cellobiosidase</term>
<term>Fungal Proteins</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Phanerochaete</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cellulose 1,4-beta-cellobiosidase</term>
<term>Nitrobenzènes</term>
<term>Phanerochaete</term>
<term>Protéines fongiques</term>
<term>Protéines recombinantes</term>
<term>Triholosides</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" qualifier="genetics" xml:lang="en"><term>Pichia</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cellulose 1,4-beta-cellobiosidase</term>
<term>Pichia</term>
<term>Protéines fongiques</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Pichia</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellulose 1,4-beta-cellobiosidase</term>
<term>Pichia</term>
<term>Protéines fongiques</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term>
<term>Catalytic Domain</term>
<term>Cloning, Molecular</term>
<term>Crystallography, X-Ray</term>
<term>Gene Expression</term>
<term>Hydrophobic and Hydrophilic Interactions</term>
<term>Models, Molecular</term>
<term>Protein Binding</term>
<term>Protein Conformation, alpha-Helical</term>
<term>Protein Conformation, beta-Strand</term>
<term>Protein Interaction Domains and Motifs</term>
<term>Substrate Specificity</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term>
<term>Cristallographie aux rayons X</term>
<term>Domaine catalytique</term>
<term>Expression des gènes</term>
<term>Interactions hydrophobes et hydrophiles</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Motifs d'acides aminés</term>
<term>Motifs et domaines d'intéraction protéique</term>
<term>Spécificité du substrat</term>
<term>Structure en brin bêta</term>
<term>Structure en hélice alpha</term>
</keywords>
</textClass>
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</teiHeader>
<front><div type="abstract" xml:lang="en">Cellobiohydrolases belonging to glycoside hydrolase family 6 (CBH II, Cel6A) play key roles in the hydrolysis of crystalline cellulose. CBH II from the white-rot fungus Phanerochaete chrysosporium (PcCel6A) consists of a catalytic domain (CD) and a carbohydrate-binding module connected by a linker peptide, like other known fungal cellobiohydrolases. In the present study, the CD of PcCel6A was crystallized without ligands, and p-nitrophenyl β-D-cellotrioside (pNPG3) was soaked into the crystals. The determined structures of the ligand-free and pNPG3-soaked crystals revealed that binding of cellobiose at substrate subsites +1 and +2 induces a conformational change of the N-terminal and C-terminal loops, switching the tunnel-shaped active site from the open to the closed form.</div>
</front>
</TEI>
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<DateCompleted><Year>2017</Year>
<Month>12</Month>
<Day>04</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>01</Month>
<Day>15</Day>
</DateRevised>
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<JournalIssue CitedMedium="Internet"><Volume>73</Volume>
<Issue>Pt 7</Issue>
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<Month>Jul</Month>
<Day>01</Day>
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<Title>Acta crystallographica. Section F, Structural biology communications</Title>
<ISOAbbreviation>Acta Crystallogr F Struct Biol Commun</ISOAbbreviation>
</Journal>
<ArticleTitle>Crystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium.</ArticleTitle>
<Pagination><MedlinePgn>398-403</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1107/S2053230X17008093</ELocationID>
<Abstract><AbstractText>Cellobiohydrolases belonging to glycoside hydrolase family 6 (CBH II, Cel6A) play key roles in the hydrolysis of crystalline cellulose. CBH II from the white-rot fungus Phanerochaete chrysosporium (PcCel6A) consists of a catalytic domain (CD) and a carbohydrate-binding module connected by a linker peptide, like other known fungal cellobiohydrolases. In the present study, the CD of PcCel6A was crystallized without ligands, and p-nitrophenyl β-D-cellotrioside (pNPG3) was soaked into the crystals. The determined structures of the ligand-free and pNPG3-soaked crystals revealed that binding of cellobiose at substrate subsites +1 and +2 induces a conformational change of the N-terminal and C-terminal loops, switching the tunnel-shaped active site from the open to the closed form.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tachioka</LastName>
<ForeName>Mikako</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Nakamura</LastName>
<ForeName>Akihiko</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ishida</LastName>
<ForeName>Takuya</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Igarashi</LastName>
<ForeName>Kiyohiko</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Samejima</LastName>
<ForeName>Masahiro</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
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<Agency>Ministry of Education, Culture, Sports, Science and Technology</Agency>
<Country></Country>
</Grant>
<Grant><GrantID>G24114008</GrantID>
<Agency>Ministry of Education, Culture, Sports, Science and Technology</Agency>
<Country></Country>
</Grant>
<Grant><GrantID>24380089</GrantID>
<Agency>Japan Society for the Promotion of Science</Agency>
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   |texte=   Crystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium.
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Crystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium.

Crystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium.

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