7WRX

Structure of Deinococcus radiodurans HerA-ADP complex

Summary for 7WRX

• Entry DOI: 10.2210/pdb7wrx/pdb
• Related: 7WRW
• Descriptor: HerA, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: hexamer, atpase, reca-like, translocase, helicase
• Biological source: Deinococcus radiodurans
• Total number of polymer chains: 12
• Total formula weight: 814604.55

Authors

Cheng, K. (deposition date: 2022-01-27, release date: 2023-02-01, Last modification date: 2023-11-29)

Primary citation

Yang, J.,Sun, Y.,Wang, Y.,Hao, W.,Cheng, K.
Structural and DNA end resection study of the bacterial NurA-HerA complex.
Bmc Biol., 21:42-42, 2023

PubMed Abstract: The nuclease NurA and the ATPase/translocase HerA play a vital role in repair of double-strand breaks (DSB) during the homologous recombination in archaea. A NurA-HerA complex is known to mediate DSB DNA end resection, leading to formation of a free 3' end used to search for the homologous sequence. Despite the structures of individual archaeal types of NurA and HerA having been reported, there is limited information regarding the molecular mechanisms underlying this process. Some bacteria also possess homologs of NurA and HerA; however, the bacterial type of this complex, as well as the detailed mechanisms underlying the joining of NurA-HerA in DSB DNA end resection, remains unclear.

PubMed: 36829173
DOI: 10.1186/s12915-023-01542-0

Experimental method

X-RAY DIFFRACTION (3.40003560509 Å)