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RecR, helix-hairpin-helix
The bacterial protein RecR is an important regulator oin the RecFOR homologous recombination pathway during DNA repair. It acts with RecF and RecO forming a complex that facilitates the loading of RecA onto ssDNA. RecR is a zinc metalloprotein consisting of a N-terminal helix-hairpin-helix (HhH) motif, a middle region containing a zinc finger motif (Pfam:PF02132) and a Toprim domain (Pfam:PF13662) and a C-terminal domain comprising a Walker B motif and a C-terminal helix (Pfam:PF21175) [1,2]. This is the HhH motif found at the N-temrinal of RecR which is essential for DNA binding and association with RecO [1,2]. [1]. 23019218. RecOR complex including RecR N-N dimer and RecO monomer displays a high affinity for ssDNA. Tang Q, Gao P, Liu YP, Gao A, An XM, Liu S, Yan XX, Liang DC;. Nucleic Acids Res. 2012;40:11115-11125. [2]. 29633970. Crystal structure of RecR, a member of the RecFOR DNA-repair pathway, from Pseudomonas aeruginosa PAO1. Che S, Chen Y, Liang Y, Zhang Q, Bartlam M;. Acta Crystallogr F Struct Biol Commun. 2018;74:222-230. (from Pfam)
RecR, C-terminal
The bacterial protein RecR is an important regulator in the RecFOR homologous recombination pathway during DNA repair. It acts with RecF and RecO forming a complex that facilitates the loading of RecA onto ssDNA. RecR is a zinc metalloprotein consisting of a N-terminal helix-hairpin-helix (HhH) motif, a middle region containing a zinc finger motif (Pfam:PF02132) and a Toprim domain (Pfam:PF13662), and a C-terminal domain comprising a Walker B motif and a C-terminal helix [1,2]. This is the C-terminal domain of RecR, which has a divergent Walker B motif, suggesting a nucleotide binding site [1,2]. [1]. 23019218. RecOR complex including RecR N-N dimer and RecO monomer displays a high affinity for ssDNA. Tang Q, Gao P, Liu YP, Gao A, An XM, Liu S, Yan XX, Liang DC;. Nucleic Acids Res. 2012;40:11115-11125. [2]. 29633970. Crystal structure of RecR, a member of the RecFOR DNA-repair pathway, from Pseudomonas aeruginosa PAO1. Che S, Chen Y, Liang Y, Zhang Q, Bartlam M;. Acta Crystallogr F Struct Biol Commun. 2018;74:222-230. (from Pfam)
toprim domain-containing protein
The toprim domain is found in a wide variety of enzymes involved in nucleic acid manipulation [1]. [1]. 9722641. Toprim--a conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins. Aravind L, Leipe DD, Koonin EV;. Nucleic Acids Res 1998;26:4205-4213. (from Pfam)
RecR, Cys4-zinc finger motif
The bacterial protein RecR is an important regulator in the RecFOR homologous recombination pathway during DNA repair. It acts with RecF and RecO forming a complex that facilitates the loading of RecA onto ssDNA. RecR is a zinc metalloprotein consisting of a N-terminal helix-hairpin-helix (HhH) motif, a middle region containing a zinc finger motif and a Toprim domain (Pfam:PF13662) and a C-terminal domain comprising a Walker B motif and a C-terminal helix [1,2]. This is the zinc finger motif, which consists of four strictly conserved cysteine residues which coordinate a zinc ion. This motif is the most conserved domain in RecR proteins and plays a structural role stabilizing the 3D structure of the protein [3]. [1]. 23019218. RecOR complex including RecR N-N dimer and RecO monomer displays a high affinity for ssDNA. Tang Q, Gao P, Liu YP, Gao A, An XM, Liu S, Yan XX, Liang DC;. Nucleic Acids Res. 2012;40:11115-11125. [2]. 29633970. Crystal structure of RecR, a member of the RecFOR DNA-repair pathway, from Pseudomonas aeruginosa PAO1. Che S, Chen Y, Liang Y, Zhang Q, Bartlam M;. Acta Crystallogr F Struct Biol Commun. 2018;74:222-230. [3]. 25460918. Structural and functional characterization of Cys4 zinc finger motif in the recombination mediator protein RecR. Tang Q, Liu YP, Yan XX, Liang DC;. DNA Repair (Amst). 2014;24:10-14. (from Pfam)
recombination mediator RecR
recombination protein RecR is a recombination mediator protein in the RecFOR pathway of homologous recombinational repair
RecR mediates the initiation of recombination and recombinational repair. RecF is also required.
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