Journal
STRUCTURE
Volume 11, Issue 3, Pages 323-328Publisher
CELL PRESS
DOI: 10.1016/S0969-2126(03)00030-3
Keywords
molecular chaperone; crystal structure; peptide binding; ClpB
Funding
- NIDDK NIH HHS [R01 DK56203] Funding Source: Medline
- NIGMS NIH HHS [R01 GM65959] Funding Source: Medline
Ask authors/readers for more resources
E. coli Hsp100 ClpB can disaggregate denatured polypeptides by employing ATP hydrolysis. The ClpB N-terminal domain (ClpBN) has been proposed to play important roles in ClpB molecular chaperone activities. We have determined the crystal structure of ClpBN to 1.95 Angstrom resolution by MAD methods. The ClpBN monomer contains two subdomains that have similar folds. The crystal structure revealed a hydrophobic groove on the molecular surface. We have constructed ClpB mutants in which the hydrophobic residues within the putative peptide binding groove were replaced by glutamine. These ClpB mutants exhibited severe defects in molecular chaperone activity but retained the wild-type ATPase activity.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available