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- Title
Crystal structure of SMU.2055 protein from Streptococcus mutans and its small molecule inhibitors design and selection.
- Authors
Chen Xiaodan; Zhan Xiurong; Wu Xinyu; Zhao Chunyan; Zhao Wanghong
- Abstract
Objective The aim of this study is to analyze the three-dimensional crystal structure of SMU.2055 protein, a putative acetyltransferase from the major caries pathogen Streptococcus mutans (S. mutans). The design and selection of the structure-based small molecule inhibitors are also studied. Methods The three-dimensional crystal structure of SMU.2055 protein was obtained by structural genomics research methods of gene cloning and expression, protein purification with Ni2+- chelating affinity chromatography, crystal screening, and X-ray diffraction data collection. An inhibitor virtual model matching with its target protein structure was set up using computer-aided drug design methods, virtual screening and fine docking, and Libdock and Autodock procedures. Results The crystal of SMU.2055 protein was obtained, and its three-dimensional crystal structure was analyzed. This crystal was diffracted to a resolution of 0.23 nm. It belongs to orthorhombic space group C222!, with unit cell parameters of a=9.20 nm, b=9.46 nm, and c=19.39 nm. The asymmetric unit contained four molecules, with a solvent content of 56.7%. Moreover, five small molecule compounds, whose structure matched with that of the target protein in high degree, were designed and selected. Conclusion Protein crystallography research of 5. mutans SMU.2055 helps to understand the structures and functions of proteins from S. mutans at the atomic level. These five compounds may be considered as effective inhibitors to SMU.2055. The virtual model of small molecule inhibitors we built will lay a foundation to the anticaries research based on the crystal structure of proteins
- Publication
West China Journal of Stomatology, 2015, Vol 33, Issue 2, p182
- ISSN
1000-1182
- Publication type
Academic Journal
- DOI
10.7518/hxkq.2015.02.016