The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
- 1 January 1996
- journal article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 379 (6560), 37-45
- https://doi.org/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.Keywords
This publication has 43 references indexed in Scilit:
- GroEL structure: a new chapter on assisted foldingStructure, 1994
- Residues in chaperonin GroEL required for polypeptide binding and releaseNature, 1994
- The crystal structure of the bacterial chaperonln GroEL at 2.8 ÅNature, 1994
- Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopyNature, 1994
- Molecular Chaperones: Opening and closing the Anfinsen cageCurrent Biology, 1994
- Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein FoldingScience, 1994
- Symmetric Complexes of GroE Chaperonins as Part of the Functional CycleScience, 1994
- Polypeptide Interactions with Molecular Chaperones and their Relationship to In Vivo Protein FoldingAnnual Review of Biophysics and Biophysical Chemistry, 1994
- Molecular chaperones in protein folding: the art of avoiding sticky situationsTrends in Biochemical Sciences, 1994
- The reaction cycle of GroEL and GroES in chaperonin-assisted protein foldingNature, 1993