| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1979640 | Current Opinion in Structural Biology | 2007 | 12 Pages |
ATPases associated with various cellular activities are aptly named. They are the engines that drive processes such as protein degradation, protein refolding, σ54-dependent transcriptional activation, DNA helicase activity, DNA replication initiation, and cellular cargo transport. Recent structural information derived from biochemical studies, electron microscopy (EM), small-angle X-ray scattering (SAXS), and X-ray crystallography are beginning to show how, at an atomic level, some of these systems use the conformational changes generated during the ATP hydrolysis cycle. Structural highlights in the processes mentioned are provided by work on ClpX and p97, ClpB, PspF and NtrC, RuvBL1, DnaA and the papillomavirus E1 initiator protein and dynein. The results emphasize the versatility of the AAA+ core domain.
