%0 Generic %A Zheng, Shuping %A Zhou, Ying %A Fleming, Joy %A Zhou, Yafeng %A Zhang, Mengting %A Li, Shiliang %A Li, Honglin %A Sun, Bingqi %A Liu, Wei %A Bi, Lijun %D 2018 %T Dataset for: Structural and genetic analysis of START superfamily protein MSMEG_0129 from Mycobacterium smegmatis %U https://wiley.figshare.com/articles/dataset/Dataset_for_Structural_and_genetic_analysis_of_START_superfamily_protein_MSMEG_0129_from_i_Mycobacterium_smegmatis_i_/5933137 %R 10.6084/m9.figshare.5933137.v1 %2 https://ndownloader.figshare.com/files/10610494 %2 https://ndownloader.figshare.com/files/10610497 %2 https://ndownloader.figshare.com/files/10610500 %K Mycobacterium tuberculosis %K START domain superfamily %K Rv0164 MSMEG_0129 %K Biophysics %K Synthetic Biology %K Biochemistry %K Plant Biology %K Virology %K Receptors and Membrane Biology %K Computational Biology %K Immunology %K Neuroscience %K Cell Development, Proliferation and Death %K Molecular Biology %K Evolutionary Biology %K Signal Transduction %K Cancer Cell Biology %K Systems Biology %K Structural Biology %X 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. %I Wiley