The tertiary structure of a bacterial cellulase determined by small-angle X-ray-scattering analysis.
作者信息
Pilz I, Schwarz E, Kilburn D G, Miller R C, Warren R A, Gilkes N R
机构信息
Institut für Physikalische Chemie, Universität Graz, Austria.
出版信息
Biochem J. 1990 Oct 1;271(1):277-80. doi: 10.1042/bj2710277.
Abstract
CenA from Cellulomonas fimi is a beta-1,4-endoglucanase that binds tightly to cellulose. X-ray-scattering analyses show that the enzyme is tadpole-shaped: the previously identified catalytic and cellulose-binding domains comprise the head and tail respectively. It appears that this structural and functional organization is common to several cellulases from bacteria and fungi.
摘要
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