The crystal structure of the GroES co-chaperonin at 2.8 A resolution

J F Hunt; A J Weaver; S J Landry; L Gierasch; J Deisenhofer

doi:10.1038/379037a0

The crystal structure of the GroES co-chaperonin at 2.8 A resolution

Nature. 1996 Jan 4;379(6560):37-45. doi: 10.1038/379037a0.

Authors

J F Hunt¹, A J Weaver, S J Landry, L Gierasch, J Deisenhofer

Affiliation

¹ Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235, USA.

PMID: 8538739
DOI: 10.1038/379037a0

Abstract

The GroES heptamer forms a dome, approximately 75 A in diameter and 30 A high, with an 8 A orifice in the centre of its roof. The 'mobile loop' segment, previously identified as a GroEL binding determinant, is disordered in the crystal structure in six subunits; the single well-ordered copy extends from the bottom outer rim of the GroES dome, suggesting that the cavity within the dome is continuous with the polypeptide binding chamber of GroEL in the chaperonin complex.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Amino Acid Sequence
Chaperonin 10 / chemistry*
Chaperonin 10 / physiology
Computer Graphics
Crystallography, X-Ray
Molecular Sequence Data
Protein Conformation
Protein Folding
Protein Structure, Secondary

Substances

Chaperonin 10