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PMID: 9584617 Published · ppublish English Journal Article Review

The ins and outs of a molecular chaperone machine.

Trends in biochemical sciences ·Vol. 23 ·No. 4 ·1998-04-00 ·Pages 138-43

Richardson A, Landry SJ, Georgopoulos C

Abstract

Genetic and biochemical work has highlighted the biological importance of the GroEL/GroES (Hsp60/Hsp10; cpn60/cpn10) chaperone machine in protein folding. GroEL's donut-shaped structure has attracted the attention of structural biologists because of its elegance as well as the secrets (substrates) it can hide. The recent determination of the GroES and GroEL/GroES structures provides a glimpse of their plasticity, revealing dramatic conformational changes that point to an elaborate mechanism, coupling ATP hydrolysis to substrate release by GroEL.

MeSH Terms
Bacteriophage T4/genetics,metabolism Escherichia coli/genetics,metabolism Models, Molecular Molecular Chaperones/chemistry,genetics,metabolism Protein Conformation Protein Folding
Chemicals
Molecular Chaperones
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Richardson A
Département de Biochimie Médicale, Université de Genève, Switzerland. [email protected]
Landry S J
Georgopoulos C
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
Published
1998-04-00
Pages
138-43
Language
English
Region
England
NLM ID
7610674
Subset
IM
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