[논문]Crystal Structure of SAV0927 and Its Functional Implications

Jeong, Soyeon; Kim, Hyo Jung; Ha, Nam-Chul; Kwon, Ae-Ran

doi:10.4014/jmb.1812.12040

[국내논문] Crystal Structure of SAV0927 and Its Functional Implications 원문보기

Journal of microbiology and biotechnology, v.29 no.3, 2019년, pp.500 - 505

Jeong, Soyeon (Department of Agricultural Biotechnology, Center for Food Safety and Toxicology, Center for Food and Bioconvergence, Research Institute for Agriculture and Life Sciences, Seoul National University) , Kim, Hyo Jung (Centre for Biomolecular Sciences, School of Pharmacy, University of Nottingham) , Ha, Nam-Chul (Department of Agricultural Biotechnology, Center for Food Safety and Toxicology, Center for Food and Bioconvergence, Research Institute for Agriculture and Life Sciences, Seoul National University) , Kwon, Ae-Ran (Department of Herbal Skin Care, College of Herbal Bioindustry, Daegu Haany University)

Abstract ▼ AI-Helper

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 $2.5{\AA}$ resolution. The protein was primarily dimeric both in solution and in the crystals. The asymmetric unit contained five dimers that are stacked linearly with ${\sim}80^{\circ}$ 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.

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aureus at the proteomic scale might be required. This study will be helpful in understanding the full features of S. aureus.

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Initial crystallization trials of the SAV0927 protein were performed using an automated crystal screening device (Mosquito) at 14℃ with the sitting-drop vapor-diffusion method. Five matrix screening solutions (MCSG-1T/ 2T/3T/4T, Anatrace and HR-110/112, Hampton Research Crystal Screen) that are commercially available were selected. The protein solution (0.
1. The purified SAV0927 protein.

성능/효과

To gain functional insights, we used the STRING database, which is a bioinformatics tool that presents known and predicted protein-protein interactions [12]. The STRING predicted that SAV0927 might be functionally related to SAV0928, SAV1496, SAV1289, SAV1290, SAV1015, NagD, SAV1430, SAV0939, FtsL, and SAV1877, although the function of none of these has been confirmed experimentally (Fig. 5). All of these proteins are hypothetical and functionally uncharacterized except NagD and FtsL.

참고문헌 (16)

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[국내논문] Crystal Structure of SAV0927 and Its Functional Implications 원문보기

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[국내논문] Crystal Structure of SAV0927 and Its Functional Implications 원문보기

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