8K3F

Crystal structure of the recombination mediator protein RecR from Campylobacter jejuni

Summary for 8K3F

• Entry DOI: 10.2210/pdb8k3f/pdb
• Descriptor: Recombination protein RecR, ZINC ION (3 entities in total)
• Functional Keywords: recombination mediator protein, recombination
• Biological source: Campylobacter jejuni
• Total number of polymer chains: 4
• Total formula weight: 88627.91

Authors

Lee, S.J.,Yoon, S.I. (deposition date: 2023-07-15, release date: 2023-11-01)

Primary citation

Lee, S.J.,Ahn, S.Y.,Oh, H.B.,Kim, S.Y.,Song, W.S.,Yoon, S.I.
Structural and Biochemical Analysis of the Recombination Mediator Protein RecR from Campylobacter jejuni.
Int J Mol Sci, 24:-, 2023

PubMed Abstract: The recombination mediator complex RecFOR, consisting of the RecF, RecO, and RecR proteins, is needed to initiate homologous recombination in bacteria by positioning the recombinase protein RecA on damaged DNA. Bacteria from the phylum Campylobacterota, such as the pathogen , lack the gene and trigger homologous recombination using only RecR and RecO. To elucidate the functional properties of RecR (cjRecR) in recombination initiation that differ from or are similar to those in RecF-expressing bacteria, we determined the crystal structure of cjRecR and performed structure-based binding analyses. cjRecR forms a rectangular ring-like tetrameric structure and coordinates a zinc ion using four cysteine residues, as observed for RecR proteins from RecF-expressing bacteria. However, the loop of RecR that has been shown to recognize RecO and RecF in RecF-expressing bacteria is substantially shorter in cjRecR as a canonical feature of Campylobacterota RecR proteins, indicating that cjRecR lost a part of the loop in evolution due to the lack of RecF and has a low RecO-binding affinity. Furthermore, cjRecR features a larger positive patch and exhibits substantially higher ssDNA-binding affinity than RecR from RecF-expressing bacteria. Our study provides a framework for a deeper understanding of the RecOR-mediated recombination pathway.

PubMed: 37629127
DOI: 10.3390/ijms241612947

Experimental method

X-RAY DIFFRACTION (2.603 Å)