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7DOG

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

Summary for 7DOG
Entry DOI10.2210/pdb7dog/pdb
DescriptorNuclease SbcCD subunit D, MANGANESE (II) ION (2 entities in total)
Functional Keywordsdna nuclease, endonuclease, exonuclease, dna repair, hydrolase
Biological sourceStaphylococcus aureus subsp. aureus Mu50
Total number of polymer chains2
Total formula weight73859.36
Authors
Lee, J.,Ha, N.-C. (deposition date: 2020-12-14, release date: 2021-05-05, Last modification date: 2023-11-29)
Primary citationLee, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.91 Å)
Structure validation

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