Three-dimensional structure of a thermostable bacterial cellulase

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...

Full description

Saved in:
Bibliographic Details
Published in:Nature (London) 1992-05, Vol.357 (6373), p.89-91
Main Authors: Juy, Michel, Amrt, Adolfo G, Alzari, Pedro M, Poljak, Roberta J, Claeyssens, Marc, Béguin, Pierre, Aubert, Jean-Paul
Format: Article
Language:English
Subjects:
Biochemistry
Biochemistry, Molecular Biology
Bioinformatics
Biological and medical sciences
Biological Physics
Cellular Biology
cellulase
Chemical Sciences
Clostridium thermocellum
Computer Science
Cristallography
Fundamental and applied biological sciences. Psychology
Humanities and Social Sciences
letter
Life Sciences
Molecular biophysics
multidisciplinary
Physics
Science
Science (multidisciplinary)
Structural Biology
structure
Structure in molecular biology
Tridimensional structure
X-ray crystallography
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/357089a0