CRYSTAL-STRUCTURE OF A CHOLERA TOXIN-RELATED HEAT-LABILE ENTEROTOXIN FROM ESCHERICHIA-COLI

被引：485
|
作者：
SIXMA, TK [1 ]
PRONK, SE [1 ]
KALK, KH [1 ]
WARTNA, ES [1 ]
VANZANTEN, BAM [1 ]
WITHOLT, B [1 ]
HOL, WGJ [1 ]
机构：
[1] STATE UNIV GRONINGEN, DEPT CHEM, BIOCHEM LAB, 9747 AG GRONINGEN, NETHERLANDS
来源：
NATURE | 1991年 / 351卷 / 6325期
关键词：
D O I：
10.1038/351371a0
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Examination of the structure of Escherichia coli heat-labile enterotoxin in the AB5 complex at a resolution of 2.3 angstrom reveals that the doughnut-shaped B pentamer binds the enzymatic A subunit using a hairpin of the A2 fragment, through a highly charged central pore. Putative ganglioside G(M1-) binding sites on the B subunits are more than 20 angstrom removed from the membrane-crossing A1 subunit. This ADP-ribosylating (A1) fragment of the toxin has structural homology with the catalytic region of exotoxin A and hence also to diphtheria toxin.
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页码：371 / 377
页数：7
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