%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