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From Proteopedia
Crystal structure of E. coli RdgC
Structural highlights
FunctionRDGC_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 PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Escherichia coli | Large Structures | Briggs GS | Emsley J | Lloyd RG | McEwan PA | Moore T | Yu J
