1v1q

From Proteopedia

Revision as of 15:13, 5 November 2007

CRYSTAL STRUCTURE OF PRIB- A PRIMOSOMAL DNA REPLICATION PROTEIN OF ESCHERICHIA COLI

Overview

PriB is one of the Escherichia coli varphiX-type primosome proteins that, are required for assembly of the primosome, a mobile multi-enzyme complex, responsible for the initiation of DNA replication. Here we report the, crystal structure of the E. coli PriB at 2.1 A resolution by, multi-wavelength anomalous diffraction using a mercury derivative. The, polypeptide chain of PriB is structurally similar to that of, single-stranded DNA-binding protein (SSB). However, the biological unit of, PriB is a dimer, not a homotetramer like SSB. Electrophoretic mobility, shift assays demonstrated that PriB binds single-stranded DNA and, single-stranded RNA with comparable affinity. We also show that PriB binds, single-stranded DNA with certain base preferences. Based on the PriB, structural information and biochemical studies, we propose that the, potential tetramer formation surface and several other regions of PriB may, participate in protein-protein interaction during DNA replication. These, findings may illuminate the role of PriB in varphiX-type primosome, assembly.

About this Structure

1V1Q is a Single protein structure of sequence from Escherichia coli with CYS and CYS as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Crystal structure of PriB, a primosomal DNA replication protein of Escherichia coli., Liu JH, Chang TW, Huang CY, Chen SU, Wu HN, Chang MC, Hsiao CD, J Biol Chem. 2004 Nov 26;279(48):50465-71. Epub 2004 Sep 21. PMID:15383524

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