Journal
CELL
Volume 132, Issue 1, Pages 43-54Publisher
CELL PRESS
DOI: 10.1016/j.cell.2007.11.045
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Funding
- NIGMS NIH HHS [GM38839, GM70841, R01 GM045547, R37 GM038839-18, R01 GM038839, R37 GM038839-17, R01 GM070841, R37 GM038839, GM45547, R37 GM038839-19, R37 GM038839-16] Funding Source: Medline
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The structure of the E. coli beta clamp polymerase processivity factor has been solved in complex with primed DNA. Interestingly, the clamp directly binds the DNA duplex and also forms a crystal contact with the ssDNA template strand, which binds into the protein-binding pocket of the clamp. We demonstrate that these clamp-DNA interactions function in clamp loading, perhaps by inducing the ring to close around DNA. Clamp binding to template ssDNA may also serve to hold the clamp at a primed site after loading or during switching of multiple factors on the clamp. Remarkably, the DNA is highly tilted as it passes through the b ring. The pronounced 22 degrees angle of DNA through b may enable DNA to switch between multiple factors bound to a single clamp simply by alternating from one protomer of the ring to the other.
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