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6IY0

Crystal structure of conserved hypothetical protein SAV0927 from Staphylococcus aureus subsp. aureus Mu50

Summary for 6IY0
Entry DOI10.2210/pdb6iy0/pdb
DescriptorSAV0927, CHLORIDE ION (3 entities in total)
Functional Keywordsduf3055, sav0927, staphylococcus aureus, unknown function
Biological sourceStaphylococcus aureus
Total number of polymer chains10
Total formula weight114535.85
Authors
Jeong, S.,Ha, N.-C. (deposition date: 2018-12-12, release date: 2019-12-18, Last modification date: 2024-11-20)
Primary citationJeong, S.,Kim, H.J.,Ha, N.C.,Kwon, A.R.
Crystal Structure of SAV0927 and Its Functional Implications.
J Microbiol Biotechnol., 29:500-505, 2019
Cited by
PubMed Abstract: 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 have frequently emerged, threatening human lives significantly. Despite much research on the genetics of , many of its genes remain unknown functionally and structurally. To counteract its toxins and to prevent the antibiotic resistance of , our understanding of should be increased at the proteomic scale. SAV0927 was first sequenced in an antibiotic resistant strain. The gene is a conserved hypothetical protein, and its homologues appear to be restricted to . In this study, we determined the crystal structure of SAV0927 at 2.5 Å 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° 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.
PubMed: 30786702
DOI: 10.4014/jmb.1812.12040
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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