7F6D

Reconstruction of the HerA-NurA complex from Deinococcus radiodurans

Summary for 7F6D

• Entry DOI: 10.2210/pdb7f6d/pdb
• EMDB information: 31478
• Descriptor: NurA, HerA (2 entities in total)
• Functional Keywords: nuclease, helicase, end resection, dna repair, hydrolase
• Biological source: Deinococcus radiodurans R1; More
• Total number of polymer chains: 8
• Total formula weight: 485678.90

Authors

Xu, Y.,Xu, L.,Guo, J.,Hua, Y.,Zhao, Y. (deposition date: 2021-06-25, release date: 2022-06-29, Last modification date: 2024-06-12)

Primary citation

Xu, Y.,Xu, L.,Qin, C.,Wang, L.,Guo, J.,Hua, Y.,Zhao, Y.
Mechanisms of helicase activated DNA end resection in bacteria.
Structure, 30:1298-1306.e3, 2022

PubMed Abstract: DNA end resection mediated by the coordinated action of nuclease and helicase is a crucial step in initiating homologous recombination. The end-resection apparatus NurA nuclease and HerA helicase are present in both archaea and bacteria. Here, we report the cryo-electron microscopy structure of a bacterial HerA-NurA complex from Deinococcus radiodurans. The structure reveals a barrel-like hexameric HerA and a distinctive NurA dimer subcomplex, which has a unique extended N-terminal region (ENR) involved in bacterial NurA dimerization and activation. In addition to the long protruding linking loop and the C-terminal α helix of NurA, the flexible ENR is close to the HerA-NurA interface and divides the central channel of the DrNurA dimer into two halves, suggesting a possible mechanism of DNA end processing. In summary, this work provides new insights into the structure, assembly, and activation mechanisms of bacterial DNA end resection mediated by a minimal end-resection apparatus.

PubMed: 35841886
DOI: 10.1016/j.str.2022.06.005

Experimental method

ELECTRON MICROSCOPY (3.85 Å)