1cem: Difference between revisions

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[[Image:1cem.jpg|left|200px]]
{{Seed}}
[[Image:1cem.png|left|200px]]


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{{STRUCTURE_1cem|  PDB=1cem  |  SCENE=  }}  
{{STRUCTURE_1cem|  PDB=1cem  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_8805535}}


==About this Structure==
==About this Structure==
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[[Category: Glycosyl hydrolase]]
[[Category: Glycosyl hydrolase]]
[[Category: Glycosyltransferase]]
[[Category: Glycosyltransferase]]
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