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2o5v

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==Overview==
==Overview==
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RecF, together with RecO and RecR, belongs to a ubiquitous group of, recombination mediators (RMs) that includes eukaryotic proteins such as, Rad52 and BRCA2. RMs help maintain genome stability in the presence of DNA, damage by loading RecA-like recombinases and displacing single-stranded, DNA-binding proteins. Here, we present the crystal structure of RecF from, Deinococcus radiodurans. RecF exhibits a high degree of structural, similarity with the head domain of Rad50, but lacks its long coiled-coil, region. The structural homology between RecF and Rad50 is extensive, encompassing the ATPase subdomain and the so-called 'Lobe II' subdomain of, Rad50. The pronounced structural conservation between bacterial RecF and, evolutionarily diverged eukaryotic Rad50 implies a conserved mechanism of, DNA binding and recognition of the boundaries of double-stranded DNA, regions. The RecF structure, mutagenesis of conserved motifs and, ATP-dependent dimerization of RecF are discussed with respect to its role, in promoting presynaptic complex formation at DNA damage sites.
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RecF, together with RecO and RecR, belongs to a ubiquitous group of recombination mediators (RMs) that includes eukaryotic proteins such as Rad52 and BRCA2. RMs help maintain genome stability in the presence of DNA damage by loading RecA-like recombinases and displacing single-stranded DNA-binding proteins. Here, we present the crystal structure of RecF from Deinococcus radiodurans. RecF exhibits a high degree of structural similarity with the head domain of Rad50, but lacks its long coiled-coil region. The structural homology between RecF and Rad50 is extensive, encompassing the ATPase subdomain and the so-called 'Lobe II' subdomain of Rad50. The pronounced structural conservation between bacterial RecF and evolutionarily diverged eukaryotic Rad50 implies a conserved mechanism of DNA binding and recognition of the boundaries of double-stranded DNA regions. The RecF structure, mutagenesis of conserved motifs and ATP-dependent dimerization of RecF are discussed with respect to its role in promoting presynaptic complex formation at DNA damage sites.
==About this Structure==
==About this Structure==
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[[Category: walker a motif]]
[[Category: walker a motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:04:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:14:52 2008''

Revision as of 16:14, 21 February 2008


2o5v, resolution 1.61Å

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Recombination mediator RecF

Overview

RecF, together with RecO and RecR, belongs to a ubiquitous group of recombination mediators (RMs) that includes eukaryotic proteins such as Rad52 and BRCA2. RMs help maintain genome stability in the presence of DNA damage by loading RecA-like recombinases and displacing single-stranded DNA-binding proteins. Here, we present the crystal structure of RecF from Deinococcus radiodurans. RecF exhibits a high degree of structural similarity with the head domain of Rad50, but lacks its long coiled-coil region. The structural homology between RecF and Rad50 is extensive, encompassing the ATPase subdomain and the so-called 'Lobe II' subdomain of Rad50. The pronounced structural conservation between bacterial RecF and evolutionarily diverged eukaryotic Rad50 implies a conserved mechanism of DNA binding and recognition of the boundaries of double-stranded DNA regions. The RecF structure, mutagenesis of conserved motifs and ATP-dependent dimerization of RecF are discussed with respect to its role in promoting presynaptic complex formation at DNA damage sites.

About this Structure

2O5V is a Single protein structure of sequence from Deinococcus radiodurans with as ligand. Full crystallographic information is available from OCA.

Reference

Structural conservation of RecF and Rad50: implications for DNA recognition and RecF function., Koroleva O, Makharashvili N, Courcelle CT, Courcelle J, Korolev S, EMBO J. 2007 Feb 7;26(3):867-77. Epub 2007 Jan 25. PMID:17255941

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