Journal
CELL
Volume 106, Issue 4, Pages 429-441Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(01)00463-9
Keywords
-
Categories
Funding
- NIGMS NIH HHS [R01 GM-45547, R01 GM-38839] Funding Source: Medline
Ask authors/readers for more resources
The gamma complex, an AAA+ ATPase, is the bacterial homolog of eukaryotic replication factor C (RFC) that loads the sliding clamp (beta, homologous to PCNA) onto DNA. The 2.7/3.0 Angstrom crystal structure of gamma complex reveals a pentameric arrangement of subunits, with stoichiometry delta':gamma (3):delta. The C-terminal domains of the subunits form a circular collar that supports an asymmetric arrangement of the N-terminal ATP binding domains of the gamma motor and the structurally related domains of the delta' stator and the delta wrench. The structure suggests a mechanism by which the gamma complex switches between a closed state, in which the beta -interacting element of delta is hidden by delta', and an open form similar to the crystal structure, in which delta is free to bind to beta.
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