2019 ; Vol.29-3: 500~505
|Author||Soyeon Jeong, Hyo Jung Kim, Nam-Chul Ha, Ae-Ran Kwon|
|Place of duty||Seoul National University, Republic of Korea|
|Title||Crystal Structure of SAV0927 and Its Functional Implications|
J. Microbiol. Biotechnol.2019 ;
|Abstract||Staphylococcus 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 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.|
|Key_word||SAV0927, DUF3055, Staphylococcus aureus, MRSA, X-ray crystallography|
Kuroda M, Ohta T, Uchiyama I, Baba T, Yuzawa H, Kobayashi I, et al. 2001. Whole genome sequencing of meticillin-resistant Staphylococcus aureus. Lancet 357:1225-1240.
Archer GL. 1998. Staphylococcus aureus: a well-armed pathogen. Clin. Infect. Dis. 26: 1179-1181.
Woods C, Colice G. 2014. Methicillin-resistant Staphylococcus aureus pneumonia in adults. Expert. Rev. Respir. Med. 8: 641-651.
Harris SR, Cartwright EJ, Torok ME, Holden MT, Brown NM, Ogilvy-Stuart AL, et al. 2013. Whole-genome sequencing for analysis of an outbreak of meticillin-resistant Staphylococcus aureus: a descriptive study. Lancet Infect. Dis. 13: 130-136.
Humphreys H, Coleman DC. 2013. Whole genome sequencing and the prevention and control of meticillin-resistant Staphylococcus aureus infection. J. Hosp. Infect. 85: 85-86.
Guerrero SA, Hecht HJ, Hofmann B, Biebl H, Singh M. 2001. Production of selenomethionine-labelled proteins using simplified culture conditions and generally applicable host/vector systems. Appl. Microbiol. Biotechnol. 56: 718-723.
Park S, Ha S, Kim Y. 2017. The protein crystallography beamlines at the Pohang light source II. Biodesign 5: 30-34.
Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods. Enzymol. 276:307-326.
Emsley P, Cowtan K. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr. D, Biol. Crystallogr. 60:2126-2132.
Adams PD, Afonine PV, Bunkoczi G, Chen VB, Davis IW, Echols N, et al. 2010. PHENIX: a comprehensive Pythonbased system for macromolecular structure solution. Acta Crystallogr. D, Biol. Crystallogr. 66: 213-221.
Holm L, Laakso LM. 2016. Dali server update. Nucleic Acids Res. 44: W351-355.
Szklarczyk D, Morris JH, Cook H, Kuhn M, Wyder S, Simonovic M, et al. 2017. The STRING database in 2017:quality-controlled protein-protein association networks, made broadly accessible. Nucleic Acids Res. 45: D362-D368.
Tremblay LW, Dunaway-Mariano D, Allen KN. 2006. Structure and activity analyses of Escherichia coli K-12 NagD provide insight into the evolution of biochemical function in the haloalkanoic acid dehalogenase superfamily. Biochemistry 45: 1183-1193.
Condon SGF, Mahbuba DA, Armstrong CR, Diaz-Vazquez G, Craven SJ, LaPointe LM, et al. 2018. The FtsLB subcomplex of the bacterial divisome is a tetramer with an uninterrupted FtsL helix linking the transmembrane and periplasmic regions. J. Biol. Chem. 293: 1623-1641.
Sievers J, Errington J. 2000. The Bacillus subtilis cell division protein FtsL localizes to sites of septation and interacts with DivIC. Mol. Microbiol. 36: 846-855.
Monteiro JM, Pereira AR, Reichmann NT, Saraiva BM, Fernandes PB, Veiga H, et al. 2018. Peptidoglycan synthesis drives an FtsZ-treadmilling-independent step of cytokinesis. Nature 554: 528-532.