6IY0
Crystal structure of conserved hypothetical protein SAV0927 from Staphylococcus aureus subsp. aureus Mu50
Summary for 6IY0
| Entry DOI | 10.2210/pdb6iy0/pdb |
| Descriptor | SAV0927, CHLORIDE ION (3 entities in total) |
| Functional Keywords | duf3055, sav0927, staphylococcus aureus, unknown function |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 10 |
| Total formula weight | 114535.85 |
| Authors | |
| Primary citation | Jeong, 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: 30786702DOI: 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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