1VDD: Crystal Structure Of Recombinational Repair Protein Recr

Citation:
Abstract
RecR, together with RecF and RecO, facilitates RecA loading in the RecF pathway of homologous recombinational DNA repair in procaryotes. The human Rad52 protein is a functional counterpart of RecFOR. We present here the crystal structure of RecR from Deinococcus radiodurans (DR RecR). A monomer of DR RecR has a two-domain structure: the N-terminal domain with a helix-hairpin-helix (HhH) motif and the C-terminal domain with a Cys4 zinc-finger motif, a Toprim domain and a Walker B motif. Four such monomers form a ring-shaped tetramer of 222 symmetry with a central hole of 30-35 angstroms diameter. In the crystal, two tetramers are concatenated, implying that the RecR tetramer is capable of opening and closing. We also show that DR RecR binds to both dsDNA and ssDNA, and that its HhH motif is essential for DNA binding.
PDB ID: 1VDDDownload
MMDB ID: 28084
PDB Deposition Date: 2004/3/20
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Similar Structures:
Biological Unit for 1VDD: tetrameric; determined by author and by software (PISA)
Molecular Components in 1VDD
Label Count Molecule
Proteins (4 molecules)
4
Recombination Protein Recr(Gene symbol: recR)
Molecule annotation
Chemicals (9 molecules)
1
4
2
5
* Click molecule labels to explore molecular sequence information.

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