Structural highlights
Function
SBCD_STAAM SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity (By similarity).
Publication Abstract from PubMed
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 A. 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.
Crystal structure of the nuclease and capping domain of SbcD from Staphylococcus aureus.,Lee J, Jo I, Ahn J, Hong S, Jeong S, Kwon A, Ha NC J Microbiol. 2021 Apr 20. pii: 10.1007/s12275-021-1012-0. doi:, 10.1007/s12275-021-1012-0. PMID:33877576[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee J, Jo I, Ahn J, Hong S, Jeong S, Kwon A, Ha NC. Crystal structure of the nuclease and capping domain of SbcD from Staphylococcus aureus. J Microbiol. 2021 Apr 20. pii: 10.1007/s12275-021-1012-0. doi:, 10.1007/s12275-021-1012-0. PMID:33877576 doi:http://dx.doi.org/10.1007/s12275-021-1012-0
