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Crystal structure of conserved hypothetical protein SAV0927 from Staphylococcus aureus subsp. aureus Mu50Crystal structure of conserved hypothetical protein SAV0927 from Staphylococcus aureus subsp. aureus Mu50
Structural highlights
FunctionPublication Abstract from PubMedStaphylococcus aureus is a round-shaped, gram-positive bacterium that can cause numerous infectious diseases ranging from mild infections such as skin infections and food poisoning to life-threatening infections such as sepsis, endocarditis and toxic shock syndrome. Various antibiotic-resistant strains of S. aureus have frequently emerged, threatening human lives significantly. Despite much research on the genetics of S. aureus, many of its genes remain unknown functionally and structurally. To counteract its toxins and to prevent the antibiotic resistance of S. aureus, our understanding of S. aureus should be increased at the proteomic scale. SAV0927 was first sequenced in an antibiotic resistant S. aureus strain. The gene is a conserved hypothetical protein, and its homologues appear to be restricted to Firmicutes. In this study, we determined the crystal structure of SAV0927 at 2.5 A resolution. The protein was primarily dimeric both in solution and in the crystals. The asymmetric unit contained five dimers that are stacked linearly with ~80 degrees rotation by each dimer, and these interactions further continued in the crystal packing, resulting in a long linear polymer. The crystal structures, together with the network analysis, provide functional implications for the SAV0927-mediated protein network. Crystal Structure of SAV0927 and Its Functional Implications.,Jeong S, Kim HJ, Ha NC, Kwon AR J Microbiol Biotechnol. 2019 Mar 28;29(3):500-505. doi: 10.4014/jmb.1812.12040. PMID:30786702[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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