2jd3

From Proteopedia

Revision as of 15:28, 6 February 2008

PARR FROM PLASMID PB171

Overview

Accurate DNA partition at cell division is vital to all living organisms., In bacteria, this process can involve partition loci, which are found on, both chromosomes and plasmids. The initial step in Escherichia coli, plasmid R1 partition involves the formation of a partition complex between, the DNA-binding protein ParR and its cognate centromere site parC on the, DNA. The partition complex is recognized by a second partition protein, the actin-like ATPase ParM, which forms filaments required for the active, bidirectional movement of DNA replicates. Here, we present the 2.8 A, crystal structure of ParR from E. coli plasmid pB171. ParR forms a tight, dimer resembling a large family of dimeric ribbon-helix-helix (RHH)(2), site-specific DNA-binding proteins. Crystallographic and electron, microscopic data further indicate that ParR dimers assemble into a helix, structure with DNA-binding sites facing outward. Genetic and biochemical, experiments support a structural arrangement in which the centromere-like, parC DNA is wrapped around a ParR protein scaffold. This structure holds, implications for how ParM polymerization drives active DNA transport, during plasmid partition.

About this Structure

2JD3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural analysis of the ParR/parC plasmid partition complex., Moller-Jensen J, Ringgaard S, Mercogliano CP, Gerdes K, Lowe J, EMBO J. 2007 Sep 27;. PMID:17898804

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