2hpm

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2hpm, resolution 3.70Å

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Eubacterial and Eukaryotic Replicative DNA Polymerases are not Homologous: X-ray Structure of DNA Polymerase III

Overview

The crystal structure of Thermus aquaticus DNA polymerase III alpha, subunit reveals that the structure of the catalytic domain of the, eubacterial replicative polymerase is unrelated to that of the eukaryotic, replicative polymerase but rather belongs to the Polbeta-like, nucleotidyltransferase superfamily. A model of the polymerase complexed, with both DNA and beta-sliding clamp interacting with a reoriented binding, domain and internal beta binding site was constructed that is consistent, with existing biochemical data. Within the crystal, two C-terminal domains, are interacting through a surface that is larger than many dimer, interfaces. Since replicative polymerases of eubacteria and, eukaryotes/archaea are not homologous, the nature of the replicative, polymerase in the last common ancestor is unknown. Although other, possibilities have been proposed, the plausibility of a ribozyme DNA, polymerase should be considered.

About this Structure

2HPM is a Single protein structure of sequence from Thermus aquaticus with ZN, MG, CL and 3PO as ligands. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.

Reference

The structure of T. aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases., Bailey S, Wing RA, Steitz TA, Cell. 2006 Sep 8;126(5):893-904. PMID:16959569

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