7f6d
From Proteopedia
Reconstruction of the HerA-NurA complex from Deinococcus radiodurans
Structural highlights
FunctionPublication Abstract from PubMedDNA 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 alpha 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. Mechanisms of helicase activated DNA end resection in bacteria.,Xu Y, Xu L, Qin C, Wang L, Guo J, Hua Y, Zhao Y Structure. 2022 Sep 1;30(9):1298-1306.e3. doi: 10.1016/j.str.2022.06.005. Epub , 2022 Jul 15. PMID:35841886[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Deinococcus radiodurans R1 | Large Structures | Guo J | Hua Y | Xu L | Xu Y | Zhao Y