1w3s

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==Overview==
==Overview==
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The RecFOR pathway has been shown to be essential for DNA repair through, the process of homologous recombination in bacteria and, recently, to be, important in the recovery of stalled replication forks following UV, irradiation. RecO, along with RecR, RecF, RecQ and RecJ, is a principal, actor in this fundamental DNA repair pathway. Here we present the, three-dimensional structure of a member of the RecO family. The crystal, structure of Deinococcus radiodurans RecO (drRecO) reveals possible, binding sites for DNA and for the RecO-binding proteins within its three, discrete structural regions: an N-terminal, oligonucleotide/oligosaccharide-binding domain, a helical bundle and a, zinc-finger motif. Furthermore, drRecO was found to form a stable complex, with RecR and to bind both single- and double-stranded DNA. Mutational, analysis confirmed the existence of multiple DNA-binding sites within the, protein.
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The RecFOR pathway has been shown to be essential for DNA repair through the process of homologous recombination in bacteria and, recently, to be important in the recovery of stalled replication forks following UV irradiation. RecO, along with RecR, RecF, RecQ and RecJ, is a principal actor in this fundamental DNA repair pathway. Here we present the three-dimensional structure of a member of the RecO family. The crystal structure of Deinococcus radiodurans RecO (drRecO) reveals possible binding sites for DNA and for the RecO-binding proteins within its three discrete structural regions: an N-terminal oligonucleotide/oligosaccharide-binding domain, a helical bundle and a zinc-finger motif. Furthermore, drRecO was found to form a stable complex with RecR and to bind both single- and double-stranded DNA. Mutational analysis confirmed the existence of multiple DNA-binding sites within the protein.
==About this Structure==
==About this Structure==
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[[Category: Deinococcus radiodurans]]
[[Category: Deinococcus radiodurans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hall, D.R.]]
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[[Category: Hall, D R.]]
[[Category: Leiros, I.]]
[[Category: Leiros, I.]]
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[[Category: Leonard, G.A.]]
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[[Category: Leonard, G A.]]
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[[Category: Mcsweeney, S.M.]]
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[[Category: Mcsweeney, S M.]]
[[Category: Timmins, J.]]
[[Category: Timmins, J.]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: sad]]
[[Category: sad]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:19:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:40:08 2008''

Revision as of 13:40, 21 February 2008


1w3s, resolution 2.40Å

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THE CRYSTAL STRUCTURE OF RECO FROM DEINOCOCCUS RADIODURANS.

Overview

The RecFOR pathway has been shown to be essential for DNA repair through the process of homologous recombination in bacteria and, recently, to be important in the recovery of stalled replication forks following UV irradiation. RecO, along with RecR, RecF, RecQ and RecJ, is a principal actor in this fundamental DNA repair pathway. Here we present the three-dimensional structure of a member of the RecO family. The crystal structure of Deinococcus radiodurans RecO (drRecO) reveals possible binding sites for DNA and for the RecO-binding proteins within its three discrete structural regions: an N-terminal oligonucleotide/oligosaccharide-binding domain, a helical bundle and a zinc-finger motif. Furthermore, drRecO was found to form a stable complex with RecR and to bind both single- and double-stranded DNA. Mutational analysis confirmed the existence of multiple DNA-binding sites within the protein.

About this Structure

1W3S is a Single protein structure of sequence from Deinococcus radiodurans with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Crystal structure and DNA-binding analysis of RecO from Deinococcus radiodurans., Leiros I, Timmins J, Hall DR, McSweeney S, EMBO J. 2005 Mar 9;24(5):906-18. Epub 2005 Feb 17. PMID:15719017

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