The lid that shapes the pot: Structure and function of the chaperonin GroES

被引:17
作者
Saibil, H
机构
[1] Department of Crystallography, Birkbeck College
关键词
D O I
10.1016/S0969-2126(96)00002-0
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 structure of GroES reveals a potential for instability at odds with the idea of a fixed ring whose only flexible regions are at the outer edges. The importance of GroES in chaperoned protein folding is highlighted by evidence that folding substrates are transiently enclosed under the GroES cap.
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页码:1 / 4
页数:4
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共 22 条
[21]   2 LINES OF ALLOSTERIC COMMUNICATION IN THE OLIGOMERIC CHAPERONIN GROEL ARE REVEALED BY THE SINGLE MUTATION ARG196-]ALA [J].
YIFRACH, O ;
HOROVITZ, A .
JOURNAL OF MOLECULAR BIOLOGY, 1994, 243 (03) :397-401
[22]   MONOMER-HEPTAMER EQUILIBRIUM OF THE ESCHERICHIA-COLI CHAPERONIN GROES [J].
ZONDLO, J ;
FISHER, KE ;
LIN, ZL ;
DUCOTE, KR ;
EISENSTEIN, E .
BIOCHEMISTRY, 1995, 34 (33) :10334-10339