2owl | pdb_00002owl

Crystal structure of E. coli RdgC

spinqualitylabelsall models 2owl, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2owl is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: CA, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RDGC_ECOLI May be involved in recombination. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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