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- Crystal structure of the nuclease and capping domain of SbcD from Staphylococcus aureus
- Jinwook Lee , Inseong Jo , Jinsook Ahn , Seokho Hong , Soyeon Jeong , Aeran Kwon , Nam-Chul Ha
- J. Microbiol. 2021;59(6):584-589. Published online April 20, 2021
- DOI: https://doi.org/10.1007/s12275-021-1012-0
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Abstract
- The SbcCD complex is an essential component of the DNA double-strand break (DSB) repair system in bacteria. The bacterial SbcCD complex recognizes and cleaves the DNA ends in DSBs by ATP-dependent endo- and exonuclease activities as an early step of the DNA repair process. SbcD consists of nuclease, capping, and helix-loop-helix domains. Here, we present the crystal structure of a SbcD fragment from Staphylococcus aureus, which contained nuclease and capping domains, at a resolution of 2.9 Å. This structure shows a dimeric assembly similar to that of the corresponding domains of SbcD from Escherichia coli. The S. aureus SbcD fragment exhibited endonuclease activities on supercoiled DNA and exonuclease activity on linear and nicked DNA. This study contributes to the understanding of the molecular basis for how bacteria can resist sterilizing treatment, causing DNA damage.
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Citations
Citations to this article as recorded by
- Staphylococcus aureus SOS response: Activation, impact, and drug targets
Kaiying Cheng, Yukang Sun, Huan Yu, Yingxuan Hu, Yini He, Yuanyuan Shen
mLife.2024; 3(3): 343. CrossRef
- Staphylococcus aureus SOS response: Activation, impact, and drug targets
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