3bep

From Proteopedia

Revision as of 15:29, 6 February 2008

Structure of a sliding clamp on DNA

Overview

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 beta ring. The, pronounced 22 degrees angle of DNA through beta 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.

About this Structure

3BEP is a Protein complex structure of sequences from Escherichia coli with as ligand. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structure of a sliding clamp on DNA., Georgescu RE, Kim SS, Yurieva O, Kuriyan J, Kong XP, O'Donnell M, Cell. 2008 Jan 11;132(1):43-54. PMID:18191219

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