1vdd
From Proteopedia
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Crystal structure of recombinational repair protein RecR
Overview
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.
About this Structure
1VDD is a Single protein structure of sequence from Deinococcus radiodurans with ZN and IMD as ligands. Full crystallographic information is available from OCA.
Reference
Ring-shaped architecture of RecR: implications for its role in homologous recombinational DNA repair., Lee BI, Kim KH, Park SJ, Eom SH, Song HK, Suh SW, EMBO J. 2004 May 19;23(10):2029-38. Epub 2004 Apr 29. PMID:15116069
Page seeded by OCA on Wed Nov 21 04:36:02 2007
