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Three-dimensional structure of a thermostable bacterial cellulase
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Three-dimensional structure of a thermostable bacterial cellulase
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Journal Article
Three-dimensional structure of a thermostable bacterial cellulase
1992
Overview
CELLULOSIC biomass is recycled by a variety of microorganisms occupying different habitats
1
. Studies of their cellulase systems have included the purification of enzyme components, the determination of their enzymological properties
2
and the cloning and characterization of their structural genes
3
. Sequence analysis of more than 70 cellulases permits grouping into seven families corresponding to distinct structural types
4,5
. The three-dimensional structure of the catalytic core of cellobiohydrolase CBHII from the fungus
Trichoderma
reesei has been reported
6
. Here we show that endoglucanase CelD from
Clostridium thermocellum
, which is representative of a different family of cellulose-degrading enzymes consisting of at least 11 bacterial, fungal and plant endoglucanases
5,7
, has a globular structure, with an amino-terminal immunoglobulin-like domain tightly packed against a larger catalytic domain. The latter shows a novel protein fold, shaped like an α-barrel of 12 helices connected by loops that form the active site. The structure of a complex CelD with a substrate analogue suggests a mechanism for substrate hydrolysis.
Publisher
Nature Publishing Group UK,Nature Publishing,Nature Publishing Group
