Structural and genetic analysis of START superfamily protein MSMEG_0129 from Mycobacterium smegmatis
Zheng S, Zhou Y, Fleming J, Zhou Y, Zhang M, Li S, Li H, Sun B, et al. (10 authors)
FEBS letters · 2018-04
Abstract
Mycobacterium tuberculosis is a notorious pathogen that continues to threaten human health. Rv0164, an antigen of both T- and B cells conserved across 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 demonstrate 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 during mycobacterial growth, for example, in lipid transfer during cell envelope synthesis.
MeSH terms
- Mycobacterium smegmatis
- Bacterial Proteins
- Crystallography, X-Ray
- Polyketides
- Molecular Docking Simulation