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1u5k
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(New page: 200px<br /><applet load="1u5k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u5k, resolution 2.00Å" /> '''Recombinational repa...)
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Revision as of 01:13, 25 November 2007
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Recombinational repair protein RecO
Overview
Recovery of arrested replication requires coordinated action of DNA, repair, replication, and recombination machineries. Bacterial RecO protein, is a member of RecF recombination repair pathway important for replication, recovery. RecO possesses two distinct activities in vitro, closely, resembling those of eukaryotic protein Rad52: DNA annealing and, RecA-mediated DNA recombination. Here we present the crystal structure of, the RecO protein from the extremely radiation resistant bacteria, Deinococcus radiodurans (DrRecO) and characterize its DNA binding and, strand annealing properties. The RecO structure is totally different from, the Rad52 structure. DrRecO is comprised of three structural domains: an, N-terminal domain which adopts an OB-fold, a novel alpha-helical domain, and an unusual zinc-binding domain. Sequence alignments suggest that the, multidomain architecture is conserved between RecO proteins from other, bacterial species and is suitable to elucidate sites of protein-protein, and DNA-protein interactions necessary for RecO functions during the, replication recovery and DNA repair.
About this Structure
1U5K is a Single protein structure of sequence from Deinococcus radiodurans r1 with ZN as ligand. Full crystallographic information is available from OCA.
Reference
A novel structure of DNA repair protein RecO from Deinococcus radiodurans., Makharashvili N, Koroleva O, Bera S, Grandgenett DP, Korolev S, Structure. 2004 Oct;12(10):1881-9. PMID:15458636
Page seeded by OCA on Sun Nov 25 03:21:02 2007
