PhanerochaeteV1, Main, Exploration, bibRecord, 000644

Crystal structure of glycoside hydrolase family 55 {beta}-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium.

Identifieur interne : 000644 ( Main/Exploration ); précédent : 000643; suivant : 000645

Crystal 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 Samejima

Source :

The Journal of biological chemistry [ 0021-9258 ] ; 2009.

RBID : pubmed:19193645

Descripteurs français

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

Affiliations:

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

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Le document en format XML

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<term>Cristallographie aux rayons X (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Glucan 1,3-beta-glucosidase (composition chimique)</term>
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<term>Phanerochaete (enzymologie)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Sites de fixation (MeSH)</term>
<term>Spécificité du substrat (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>bêta-Glucanes (composition chimique)</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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<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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Crystal structure of glycoside hydrolase family 55 {beta}-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium.

Crystal structure of glycoside hydrolase family 55 {beta}-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium.

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