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1u5k

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[[Image:1u5k.jpg|left|200px]]
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{{STRUCTURE_1u5k| PDB=1u5k | SCENE= }}
{{STRUCTURE_1u5k| PDB=1u5k | SCENE= }}
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'''Recombinational repair protein RecO'''
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===Recombinational repair protein RecO===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15458636 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15458636}}
==About this Structure==
==About this Structure==
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[[Category: Obd-fold]]
[[Category: Obd-fold]]
[[Category: Zn-binding]]
[[Category: Zn-binding]]
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Revision as of 21:47, 28 July 2008

Image:1u5k.png

Template:STRUCTURE 1u5k

Recombinational repair protein RecO

Template:ABSTRACT PUBMED 15458636

About this Structure

1U5K is a Single protein structure of sequence from Deinococcus radiodurans r1. 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

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