Crystal structure of glycoside hydrolase family 55 {beta}-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium.
Identifieur interne : 000646 ( Main/Curation ); précédent : 000645; suivant : 000647Crystal structure of glycoside hydrolase family 55 {beta}-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium.
Auteurs : Takuya Ishida [Japon] ; Shinya Fushinobu ; Rie Kawai ; Motomitsu Kitaoka ; Kiyohiko Igarashi ; Masahiro SamejimaSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2009.
Descripteurs français
- KwdFr :
- Catalyse (MeSH), Cinétique (MeSH), Conformation moléculaire (MeSH), Cristallographie aux rayons X (MeSH), Données de séquences moléculaires (MeSH), Glucan 1,3-beta-glucosidase (composition chimique), Hydrolyse (MeSH), Modèles moléculaires (MeSH), Peptides (composition chimique), Phanerochaete (enzymologie), Similitude de séquences d'acides aminés (MeSH), Sites de fixation (MeSH), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH), bêta-Glucanes (composition chimique).
- MESH :
- composition chimique : Glucan 1,3-beta-glucosidase, Peptides, bêta-Glucanes.
- enzymologie : Phanerochaete.
- Catalyse, Cinétique, Conformation moléculaire, Cristallographie aux rayons X, Données de séquences moléculaires, Hydrolyse, Modèles moléculaires, Similitude de séquences d'acides aminés, Sites de fixation, Spécificité du substrat, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Binding Sites (MeSH), Catalysis (MeSH), Crystallography, X-Ray (MeSH), Glucan 1,3-beta-Glucosidase (chemistry), Hydrolysis (MeSH), Kinetics (MeSH), Models, Molecular (MeSH), Molecular Conformation (MeSH), Molecular Sequence Data (MeSH), Peptides (chemistry), Phanerochaete (enzymology), Sequence Homology, Amino Acid (MeSH), Substrate Specificity (MeSH), beta-Glucans (chemistry).
- MESH :
- chemical , chemistry : Glucan 1,3-beta-Glucosidase, Peptides, beta-Glucans.
- enzymology : Phanerochaete.
- Amino Acid Sequence, Binding Sites, Catalysis, Crystallography, X-Ray, Hydrolysis, Kinetics, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Sequence Homology, Amino Acid, Substrate Specificity.
Abstract
Glycoside hydrolase family 55 consists of beta-1,3-glucanases mainly from filamentous fungi. A beta-1,3-glucanase (Lam55A) from the Basidiomycete Phanerochaete chrysosporium hydrolyzes beta-1,3-glucans in the exo-mode with inversion of anomeric configuration and produces gentiobiose in addition to glucose from beta-1,3/1,6-glucans. Here we report the crystal structure of Lam55A, establishing the three-dimensional structure of a member of glycoside hydrolase 55 for the first time. Lam55A has two beta-helical domains in a single polypeptide chain. These two domains are separated by a long linker region but are positioned side by side, and the overall structure resembles a rib cage. In the complex, a gluconolactone molecule is bound at the bottom of a pocket between the two beta-helical domains. Based on the position of the gluconolactone molecule, Glu-633 appears to be the catalytic acid, whereas the catalytic base residue could not be identified. The substrate binding pocket appears to be able to accept a gentiobiose unit near the cleavage site, and a long cleft runs from the pocket, in accordance with the activity of this enzyme toward various beta-1,3-glucan oligosaccharides. In conclusion, we provide important features of the substrate-binding site at the interface of the two beta-helical domains, demonstrating an unexpected variety of carbohydrate binding modes.
DOI: 10.1074/jbc.M808122200
PubMed: 19193645
PubMed Central: PMC2665064
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pubmed:19193645Le document en format XML
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<term>Spécificité du substrat (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<front><div type="abstract" xml:lang="en">Glycoside hydrolase family 55 consists of beta-1,3-glucanases mainly from filamentous fungi. A beta-1,3-glucanase (Lam55A) from the Basidiomycete Phanerochaete chrysosporium hydrolyzes beta-1,3-glucans in the exo-mode with inversion of anomeric configuration and produces gentiobiose in addition to glucose from beta-1,3/1,6-glucans. Here we report the crystal structure of Lam55A, establishing the three-dimensional structure of a member of glycoside hydrolase 55 for the first time. Lam55A has two beta-helical domains in a single polypeptide chain. These two domains are separated by a long linker region but are positioned side by side, and the overall structure resembles a rib cage. In the complex, a gluconolactone molecule is bound at the bottom of a pocket between the two beta-helical domains. Based on the position of the gluconolactone molecule, Glu-633 appears to be the catalytic acid, whereas the catalytic base residue could not be identified. The substrate binding pocket appears to be able to accept a gentiobiose unit near the cleavage site, and a long cleft runs from the pocket, in accordance with the activity of this enzyme toward various beta-1,3-glucan oligosaccharides. In conclusion, we provide important features of the substrate-binding site at the interface of the two beta-helical domains, demonstrating an unexpected variety of carbohydrate binding modes.</div>
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<ArticleTitle>Crystal structure of glycoside hydrolase family 55 {beta}-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium.</ArticleTitle>
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<Abstract><AbstractText>Glycoside hydrolase family 55 consists of beta-1,3-glucanases mainly from filamentous fungi. A beta-1,3-glucanase (Lam55A) from the Basidiomycete Phanerochaete chrysosporium hydrolyzes beta-1,3-glucans in the exo-mode with inversion of anomeric configuration and produces gentiobiose in addition to glucose from beta-1,3/1,6-glucans. Here we report the crystal structure of Lam55A, establishing the three-dimensional structure of a member of glycoside hydrolase 55 for the first time. Lam55A has two beta-helical domains in a single polypeptide chain. These two domains are separated by a long linker region but are positioned side by side, and the overall structure resembles a rib cage. In the complex, a gluconolactone molecule is bound at the bottom of a pocket between the two beta-helical domains. Based on the position of the gluconolactone molecule, Glu-633 appears to be the catalytic acid, whereas the catalytic base residue could not be identified. The substrate binding pocket appears to be able to accept a gentiobiose unit near the cleavage site, and a long cleft runs from the pocket, in accordance with the activity of this enzyme toward various beta-1,3-glucan oligosaccharides. In conclusion, we provide important features of the substrate-binding site at the interface of the two beta-helical domains, demonstrating an unexpected variety of carbohydrate binding modes.</AbstractText>
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