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4O6P

Structural and functional studies the characterization of C58G/C70G mutant in Cys4 Zinc-finger motif in the recombination mediator protein RecR

Summary for 4O6P
Entry DOI10.2210/pdb4o6p/pdb
Related4O6O
DescriptorRecombination protein RecR, ZINC ION (3 entities in total)
Functional Keywordszinc finger, dna repair, dna binding, recombination
Biological sourceThermoanaerobacter tengcongensis
Total number of polymer chains2
Total formula weight47217.00
Authors
Tang, Q.,Liu, Y.P.,Yan, X.X.,Liang, D.C. (deposition date: 2013-12-23, release date: 2014-12-10, Last modification date: 2023-11-08)
Primary citationTang, Q.,Liu, Y.P.,Yan, X.X.,Liang, D.C.
Structural and functional characterization of Cys4 zinc finger motif in the recombination mediator protein RecR.
DNA Repair (Amst.), 24:10-14, 2014
Cited by
PubMed Abstract: Zinc finger motif widely exists in protein structure, which can play different roles in different proteins. RecR is an important recombination mediator protein (RMP) in the RecFOR pathway and zinc finger motif is the most conserved domain in RecR protein. However, the function of this zinc finger motif in RecR is unclear. Here, we have studied the structures of the single cysteine and double cysteines mutation within the zinc finger motif in Thermoanaerobacter tengcongensis RecR (TTERecR). We have also studied the DNA binding ability as well as TTERecO protein binding ability of single, double and even triple cysteines mutation of the zinc finger motif, and the mutants do not alter DNA binding by RecR nor the interaction between RecR and RecO. The function of TTERecR zinc finger motif is to maintain the stability of the three-dimensional structure.
PubMed: 25460918
DOI: 10.1016/j.dnarep.2014.09.012
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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數據於2024-11-06公開中

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