TY - DATA T1 - Dataset for: Structural and genetic analysis of START superfamily protein MSMEG_0129 from Mycobacterium smegmatis PY - 2018/04/09 AU - Shuping Zheng AU - Ying Zhou AU - Joy Fleming AU - Yafeng Zhou AU - Mengting Zhang AU - Shiliang Li AU - Honglin Li AU - Bingqi Sun AU - Wei Liu AU - Lijun Bi UR - https://wiley.figshare.com/articles/dataset/Dataset_for_Structural_and_genetic_analysis_of_START_superfamily_protein_MSMEG_0129_from_i_Mycobacterium_smegmatis_i_/5933137 DO - 10.6084/m9.figshare.5933137.v1 L4 - https://ndownloader.figshare.com/files/10610494 L4 - https://ndownloader.figshare.com/files/10610497 L4 - https://ndownloader.figshare.com/files/10610500 KW - Mycobacterium tuberculosis KW - START domain superfamily KW - Rv0164 MSMEG_0129 KW - Biophysics KW - Synthetic Biology KW - Biochemistry KW - Plant Biology KW - Virology KW - Receptors and Membrane Biology KW - Computational Biology KW - Immunology KW - Neuroscience KW - Cell Development, Proliferation and Death KW - Molecular Biology KW - Evolutionary Biology KW - Signal Transduction KW - Cancer Cell Biology KW - Systems Biology KW - Structural Biology N2 - Mycobacterium tuberculosis, a notorious pathogen, still threatens human health. Rv0164, an antigen of both T- and B-cells conserved across the mycobacteria, and MSMEG_0129, its close homolog in Mycobacterium smegmatis, are predicted members of the START domain superfamily, but their molecular function is unknown. Here, gene knockout studies demonstrated MSMEG_0129 is essential for bacterial growth, suggesting Rv0164 may be a potential drug target. The MSMEG_0129 crystal structure determined at 1.95 Å reveals a fold similar to that in polyketide aromatase/cyclases ZhuI and TcmN from Streptomyces sp.. Structural comparisons and docking simulations, however, infer that MSMEG_0129 and Rv0164 are unlikely to catalyze polyketide aromatization/cyclization, but probably play an irreplaceable role, for example in lipid transfer, in cell envelope synthesis during mycobacterial growth. ER -