1im4

From Proteopedia

Revision as of 15:22, 20 November 2007

Crystal Structure of a DinB Homolog (DBH) Lesion Bypass DNA Polymerase Catalytic Fragment from Sulfolobus solfataricus

Overview

The UmuC/DinB family of bypass polymerases is responsible for translesion, DNA synthesis and includes the human polymerases eta, iota, and kappa. We, determined the 2.3 A resolution crystal structure of a catalytic fragment, of the DinB homolog (Dbh) polymerase from Sulfolobus solfataricus and show, that it is nonprocessive and can bypass an abasic site. The structure of, the catalytic domain is nearly identical to those of most other polymerase, families. Homology modeling suggests that there is minimal contact between, protein and DNA, that the nascent base pair binding pocket is quite, accessible, and that the enzyme is already in a closed conformation, characteristic of ternary polymerase complexes. These observations afford, insights into the sources of low fidelity and low processivity of the, UmuC/DinB polymerases.

About this Structure

1IM4 is a Single protein structure of sequence from Sulfolobus solfataricus with SO4 as ligand. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.

Reference

Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain., Zhou BL, Pata JD, Steitz TA, Mol Cell. 2001 Aug;8(2):427-37. PMID:11545744

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