7DOG

Crystal structure of a nuclease and capping domain of SbcD from Staphylococcus aureus

Summary for 7DOG

• Entry DOI: 10.2210/pdb7dog/pdb
• Descriptor: Nuclease SbcCD subunit D, MANGANESE (II) ION (2 entities in total)
• Functional Keywords: dna nuclease, endonuclease, exonuclease, dna repair, hydrolase
• Biological source: Staphylococcus aureus subsp. aureus Mu50
• Total number of polymer chains: 2
• Total formula weight: 73859.36

Authors

Lee, J.,Ha, N.-C. (deposition date: 2020-12-14, release date: 2021-05-05, Last modification date: 2023-11-29)

Primary citation

Lee, J.,Jo, I.,Ahn, J.,Hong, S.,Jeong, S.,Kwon, A.,Ha, N.C.
Crystal structure of the nuclease and capping domain of SbcD from Staphylococcus aureus.
J.Microbiol, 59:584-589, 2021

PubMed 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.

PubMed: 33877576
DOI: 10.1007/s12275-021-1012-0

Experimental method

X-RAY DIFFRACTION (2.91 Å)