Structural aspects of GroEL function

被引：55

作者：

Horovitz, A ^{[1
]}

机构：

[1] Weizmann Inst Sci, Dept Biol Struct, IL-76100 Rehovot, Israel

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1998年 / 8卷 / 01期

基金：

以色列科学基金会;

关键词：

D O I：

10.1016/S0959-440X(98)80015-8

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 chaperonin GroEL and its cofactor GroES facilitate protein folding in an ATP-regulated manner. The recently solved crystal structure of the GroEL-GroES.(ADP)(7) complex shows that the lining of the cavity in the polypeptide acceptor state is hydrophobic, whereas in the protein-release state it becomes hydrophilic. Other highlights of the past year include the visualization of the allosteric states of GroEL with respect to ATP using cryo-electron microscopy, and an X-ray crystallographic analysis of the interaction between the apical domain of GroEL and a peptide.

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页码：93 / 100

页数：8

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