3VE5

Structure of recombination mediator protein RecR16-196 deletion mutant

Summary for 3VE5

• Entry DOI: 10.2210/pdb3ve5/pdb
• Related: 3VDP 3VDS 3VDT 3VDU
• Descriptor: Recombination protein recR, ZINC ION, IMIDAZOLE, ... (4 entities in total)
• Functional Keywords: hhh domain, zinc finger, dna repair, dna binding, recombination
• Biological source: Thermoanaerobacter tengcongensis
• Total number of polymer chains: 2
• Total formula weight: 43515.83

Authors

Tang, Q.,Yan, X.X.,Liang, D.C. (deposition date: 2012-01-07, release date: 2012-12-19, Last modification date: 2023-11-08)

Primary citation

Tang, Q.,Gao, P.,Liu, Y.P.,Gao, A.,An, X.M.,Liu, S.,Yan, X.X.,Liang, D.C.
RecOR complex including RecR N-N dimer and RecO monomer displays a high affinity for ssDNA
Nucleic Acids Res., 40:11115-11125, 2012

PubMed Abstract: RecR is an important recombination mediator protein in the RecFOR pathway. RecR together with RecO and RecF facilitates RecA nucleoprotein filament formation and homologous pairing. Structural and biochemical studies of Thermoanaerobacter tengcongensis RecR (TTERecR) and its series mutants revealed that TTERecR uses the N-N dimer as a basic functional unit to interact with TTERecO monomer. Two TTERecR N-N dimers form a ring-shaped tetramer via an interaction between their C-terminal regions. The tetramer is a result of crystallization only. Hydrophobic interactions between the entire helix-hairpin-helix domains within the N-terminal regions of two TTERecR monomers are necessary for formation of a RecR functional N-N dimer. The TTERecR N-N dimer conformation also affects formation of a hydrophobic patch, which creates a binding site for TTERecO in the TTERecR Toprim domain. In addition, we demonstrate that TTERecR does not bind single-stranded DNA (ssDNA) and binds double-stranded DNA very weakly, whereas TTERecOR complex can stably bind DNA, with a higher affinity for ssDNA than double-stranded DNA. Based on these results, we propose an interaction model for the RecOR:ssDNA complex.

PubMed: 23019218
DOI: 10.1093/nar/gks889

Experimental method

X-RAY DIFFRACTION (2.8 Å)