2OWL

Crystal structure of E. coli RdgC

Summary for 2OWL

• Entry DOI: 10.2210/pdb2owl/pdb
• Descriptor: Recombination-associated protein rdgC, CALCIUM ION (3 entities in total)
• Functional Keywords: recombination, replication, reca
• Biological source: Escherichia coli
• Cellular location: Cytoplasm, nucleoid: P36767
• Total number of polymer chains: 2
• Total formula weight: 69372.08

Authors

Briggs, G.S.,McEwan, P.A.,Yu, J.,Moore, T.,Emsley, J.,Lloyd, R.G. (deposition date: 2007-02-16, release date: 2007-03-20, Last modification date: 2024-10-09)

Primary citation

Briggs, G.S.,McEwan, P.A.,Yu, J.,Moore, T.,Emsley, J.,Lloyd, R.G.
Ring Structure of the Escherichia coli DNA-binding Protein RdgC Associated with Recombination and Replication Fork Repair.
J.Biol.Chem., 282:12353-12357, 2007

PubMed Abstract: The DNA-binding protein, RdgC, is associated with recombination and replication fork repair in Escherichia coli and with the virulence-associated, pilin antigenic variation mediated by RecA and other recombination proteins in Neisseria species. We solved the structure of the E. coli protein and refined it to 2.4A. RdgC crystallizes as a dimer with a head-to-head, tail-to-tail organization forming a ring with a 30 A diameter hole at the center. The protein fold is unique and reminiscent of a horseshoe with twin gates closing the open end. The central hole is lined with positively charged residues and provides a highly plausible DNA binding channel consistent with the nonspecific mode of binding detected in vitro and with the ability of RdgC to modulate RecA function in vivo.

PubMed: 17308310
DOI: 10.1074/jbc.C700023200

Experimental method

X-RAY DIFFRACTION (2.4 Å)