期刊
CELL
卷 132, 期 1, 页码 43-54出版社
CELL PRESS
DOI: 10.1016/j.cell.2007.11.045
关键词
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资金
- 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
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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