Structure and function of endoglucanase V.
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.
Department of Chemistry, University of York, Heslington, UK.
G J
GJ
Davies
G G
GG
Dodson
R E
RE
Hubbard
S P
SP
Tolley
Z
Z
Dauter
K S
KS
Wilson
C
C
Hjort
J M
JM
Mikkelsen
G
G
Rasmussen
M
M
Schülein
D001665:Binding Sites; D002480:Cellulase / Q000737:chemistry* / Q000378:metabolism; D003196:Computer Graphics; D003904:Mitosporic Fungi / Q000201:enzymology; D009113:Muramidase / Q000737:chemistry; D011487:Protein Conformation; D014961:X-Ray Diffraction
D009113:Muramidase; D002480:Cellulase