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1cem

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Revision as of 08:23, 20 March 2008 by OCA (Talk | contribs)
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PDB ID 1cem

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, resolution 1.65Å
Gene: CELA (Clostridium thermocellum)
Activity: Cellulase, with EC number 3.2.1.4
Coordinates: save as pdb, mmCIF, xml



ENDOGLUCANASE A (CELA) CATALYTIC CORE, RESIDUES 33-395


Overview

BACKGROUND. Cellulases, which catalyze the hydrolysis of glycosidic bonds in cellulose, can be classified into several different protein families. Endoglucanase CelA is a member of glycosyl hydrolase family 8, a family for which no structural information was previously available. RESULTS. The crystal structure of CelA was determined by multiple isomorphous replacement and refined to 1.65 A resolution. The protein folds into a regular (alpha/alpha)6 barrel formed by six inner and six outer alpha helices. Cello-oligosaccharides bind to an acidic cleft containing at least five D-glucosyl-binding subsites (A-E) such that the scissile glycosidic linkage lies between subsites C and D. The strictly conserved residue Glu95, which occupies the center of the substrate-binding cleft and is hydrogen bonded to the glycosidic oxygen, has been assigned the catalytic role of proton donor. CONCLUSIONS. The present analysis provides a basis for modeling homologous family 8 cellulases. The architecture of the active-site cleft, presenting at least five glucosyl-binding subsites, explains why family 8 cellulases cleave cello-oligosaccharide polymers that are at least five D-glycosyl subunits long. Furthermore, the structure of CelA allows comparison with (alpha/alpha)6 barrel glycosidases that are not related in sequence, suggesting a possible, albeit distant, evolutionary relationship between different families of glycosyl hydrolases.

About this Structure

1CEM is a Single protein structure of sequence from Clostridium thermocellum. Full crystallographic information is available from OCA.

Reference

The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum., Alzari PM, Souchon H, Dominguez R, Structure. 1996 Mar 15;4(3):265-75. PMID:8805535

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