8IOO

Crystal structure of Deinococcus radiodurans RecJ-like protein in complex with Mg2+

Summary for 8IOO

• Entry DOI: 10.2210/pdb8ioo/pdb
• Descriptor: RecJ-like protein, MAGNESIUM ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: rnase, nuclease, hydrolase
• Biological source: Deinococcus radiodurans
• Total number of polymer chains: 3
• Total formula weight: 107879.75

Authors

Cheng, K. (deposition date: 2023-03-13, release date: 2024-03-20, Last modification date: 2024-07-17)

Primary citation

Wang, Y.,Hao, W.,Guo, Z.,Sun, Y.,Wu, Y.,Sun, Y.,Gao, T.,Luo, Y.,Jin, L.,Yang, J.,Cheng, K.
Structural and functional investigation of the DHH/DHHA1 family proteins in Deinococcus radiodurans.
Nucleic Acids Res., 52:7142-7157, 2024

PubMed Abstract: DHH/DHHA1 family proteins have been proposed to play critical roles in bacterial resistance to environmental stresses. Members of the most radioresistant bacteria genus, Deinococcus, possess two DHH/DHHA1 family proteins, RecJ and RecJ-like. While the functions of Deinococcus radiodurans RecJ (DrRecJ) in DNA damage resistance have been well characterized, the role and biochemical activities of D. radiodurans RecJ-like (DrRecJ-like) remain unclear. Phenotypic and transcriptomic analyses suggest that, beyond DNA repair, DrRecJ is implicated in cell growth and division. Additionally, DrRecJ-like not only affects stress response, cell growth, and division but also correlates with the folding/stability of intracellular proteins, as well as the formation and stability of cell membranes/walls. DrRecJ-like exhibits a preferred catalytic activity towards short single-stranded RNA/DNA oligos and c-di-AMP. In contrast, DrRecJ shows no activity against RNA and c-di-AMP. Moreover, a crystal structure of DrRecJ-like, with Mg2+ bound in an open conformation at a resolution of 1.97 Å, has been resolved. Subsequent mutational analysis was conducted to pinpoint the crucial residues essential for metal cation and substrate binding, along with the dimerization state, necessary for DrRecJ-like's function. This finding could potentially extend to all NrnA-like proteins, considering their conserved amino acid sequence and comparable dimerization forms.

PubMed: 38804263
DOI: 10.1093/nar/gkae451

Experimental method

X-RAY DIFFRACTION (2 Å)