CRYSTAL-STRUCTURE OF BACILLUS-LICHENIFORMIS 1,3-1,4-BETA-D-GLUCAN 4-GLUCANOHYDROLASE AT 1.8 ANGSTROM RESOLUTION

被引:77
作者
HAHN, M
PONS, J
PLANAS, A
QUEROL, E
HEINEMANN, U
机构
[1] MAX DELBRUCK CENTRUM MOLEK MED,FORSCHUNGSGRP KRISTALLOG,D-13122 BERLIN,GERMANY
[2] UNIV RAMON LLULL,INST QUIM SARRIA,CETS,E-08017 BARCELONA,SPAIN
[3] UNIV AUTONOMA BARCELONA,INST BIOL FONAMENTAL,E-08193 BARCELONA,SPAIN
关键词
1,3-1,4-BETA-D-GLUCAN 4-GLUCANOHYDROLASE; 1,3-1,4-BETA-GLUCANASE; BACILLUS LICHENIFORMIS; CRYSTAL STRUCTURE; BETA-GLUCAN HYDROLYSIS; ENZYME MECHANISM;
D O I
10.1016/0014-5793(95)01111-Q
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
The crystal structure of the 1,3-1,4-beta-D-glucan 4-glucanohydrolase from Bacillus licheniformis is solved at a resolution of 1.8 Angstrom and refined to R = 16.5%. The protein has a similar beta-sandwich structure as the homologous enzyme from Bacillus macer rms and the hybrid H(A16-M). This demonstrates that the jellyroll fold of these proteins is remarkably rigid and only weakly influenced by crystal contacts, The crystal structure permits to extend mechanistic considerations derived for the B. licheniformis enzyme to the entire class of bacterial 1,3-1,4-beta-D-glucan 4-glucanohydrolases.
引用
收藏
页码:221 / 224
页数:4
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