Structure and function of endoglucanase V

• Published in: Nature (London) Vol. 365; no. 6444; pp. 362 - 364
• Main Authors: Davies, Gideon J, Dodson, G. Guy, Hubbard, Roderick E, Tolley, Shirley P, Dauter, Zbigniew, Wilson, Keith S, Hjort, Carsten, Mikkelsen, Jan Møller, Rasmussen, Grethe, Schülein, Martin
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 23.09.1993; Nature Publishing Group
• Subjects: Analytical, structural and metabolic biochemistry; Binding Sites; Biological and medical sciences; Cellular biology; Cellulase - chemistry; Cellulase - metabolism; Computer Graphics; Enzymes; Enzymes and enzyme inhibitors; Flowers & plants; Fundamental and applied biological sciences. Psychology; Humicola insolens; Hydrolases; Mitosporic Fungi - enzymology; Muramidase - chemistry; Protein Conformation; X-Ray Diffraction; Fungi; Active site; Cellulose; Computerized processing; Fungi Imperfecti; Heavy atom method; Secondary structure; Spatial structure; Thallophyta; Crystalline structure
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/365362a0

Cellulose is the major polysaccharide component of plant cell walls and is the most abundant organic compound on the planet. A number of bacterial and fungal organisms can use cellulose as a food source, possessing cellulases (cellobiohydrolases and endoglucanases) that can catalyse the hydrolysis of the beta-(1,4) glycosidic bonds. They can be classified into seven distinct families. The three-dimensional structures of members of two of these families are known. Here we report the structure of a third cellulase, endoglucanase V, whose sequence is not represented in any of the above families. The enzyme is structurally distinct from the previously determined cellulases but is similar to a recently characterized plant defence protein. The active site region resembles that of lysozyme, despite the lack of structural similarity between these two enzymes.