2o5v
From Proteopedia
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|PDB= 2o5v |SIZE=350|CAPTION= <scene name='initialview01'>2o5v</scene>, resolution 1.61Å | |PDB= 2o5v |SIZE=350|CAPTION= <scene name='initialview01'>2o5v</scene>, resolution 1.61Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= recF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1299 Deinococcus radiodurans]) | |GENE= recF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1299 Deinococcus radiodurans]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o5v OCA], [http://www.ebi.ac.uk/pdbsum/2o5v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2o5v RCSB]</span> | ||
}} | }} | ||
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[[Category: Korolev, S.]] | [[Category: Korolev, S.]] | ||
[[Category: Koroleva, O.]] | [[Category: Koroleva, O.]] | ||
| - | [[Category: SO4]] | ||
[[Category: abc atpase]] | [[Category: abc atpase]] | ||
[[Category: p-loop]] | [[Category: p-loop]] | ||
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[[Category: walker a motif]] | [[Category: walker a motif]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:13:09 2008'' |
Revision as of 01:13, 31 March 2008
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| , resolution 1.61Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | recF (Deinococcus radiodurans) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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