THE TERTIARY STRUCTURE OF A BACTERIAL CELLULASE DETERMINED BY SMALL-ANGLE X-RAY-SCATTERING ANALYSIS

被引：37

作者：

PILZ, I

SCHWARZ, E

KILBURN, DG

MILLER, RC

WARREN, RAJ

GILKES, NR

机构：

[1] UNIV BRITISH COLUMBIA, DEPT MICROBIOL, VANCOUVER V6T 1W5, BC, CANADA

[2] GRAZ UNIV, INST PHYS CHEM, A-8010 GRAZ, AUSTRIA

来源：

BIOCHEMICAL JOURNAL | 1990年 / 271卷 / 01期

关键词：

D O I：

10.1042/bj2710277

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

CenA from Cellulomonas fimi is a β-1,4-endoglucanase that binds tightly to cellulse 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.

引用

页码：277 / 280

页数：4

共 21 条

[1]

ABUJA PM, 1988, EUR BIOPHYS J BIOPHY, V15, P339, DOI 10.1007/BF00254721

[2] DOMAIN-STRUCTURE OF CELLOBIOHYDROLASE-II AS STUDIED BY SMALL-ANGLE X-RAY-SCATTERING - CLOSE RESEMBLANCE TO CELLOBIOHYDROLASE-I [J].