1unn | pdb_00001unn
COMPLEX OF BETA-CLAMP PROCESSIVITY FACTOR AND LITTLE FINGER DOMAIN OF POLIV
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Overview
Y-family DNA polymerases can extend primer strands across template strand, lesions that stall replicative polymerases. The poor processivity and, fidelity of these enzymes, key to their biological role, requires that, their access to the primer-template junction is both facilitated and, regulated in order to minimize mutations. These features are believed to, be provided by interaction with processivity factors, beta-clamp or, proliferating cell nuclear antigen (PCNA), which are also essential for, the function of replicative DNA polymerases. The basis for this, interaction is revealed by the crystal structure of the complex between, the 'little finger' domain of the Y-family DNA polymerase Pol IV and the, beta-clamp processivity factor, both from Escherichia coli. The main, interaction ... [(full description)]
About this Structure
1UNN is a [Protein complex] structure of sequences from [Escherichia coli] with SO4 as [ligand]. Active as [DNA-directed DNA polymerase], with EC number [2.7.7.7]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the beta-clamp., Bunting KA, Roe SM, Pearl LH, EMBO J. 2003 Nov 3;22(21):5883-92. PMID:14592985
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