2owl
From Proteopedia
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Crystal structure of E. coli RdgC
Overview
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 30A, 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.
About this Structure
2OWL is a Single protein structure of sequence from Escherichia coli with CA as ligand. Full crystallographic information is available from OCA.
Reference
Ring Structure of the Escherichia coli DNA-binding Protein RdgC Associated with Recombination and Replication Fork Repair., Briggs GS, McEwan PA, Yu J, Moore T, Emsley J, Lloyd RG, J Biol Chem. 2007 Apr 27;282(17):12353-7. Epub 2007 Feb 16. PMID:17308310
Page seeded by OCA on Wed Nov 21 13:20:35 2007
Categories: Escherichia coli | Single protein | Briggs, G.S. | Emsley, J. | Lloyd, R.G. | McEwan, P.A. | Moore, T. | Yu, J. | CA | Reca | Recombination | Replication
