Structural and genetic analysis of START superfamily protein MSMEG_0129 from Mycobacterium smegmatis

FEBS Lett. 2018 Apr;592(8):1445-1457. doi: 10.1002/1873-3468.13024. Epub 2018 Apr 11.

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.

Keywords: Mycobacterium tuberculosis; MSMEG_0129; Rv0164; START domain superfamily; structure.

Publication types

  • Letter
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins* / chemistry
  • Bacterial Proteins* / genetics
  • Bacterial Proteins* / metabolism
  • Crystallography, X-Ray
  • Molecular Docking Simulation*
  • Mycobacterium smegmatis* / enzymology
  • Mycobacterium smegmatis* / genetics
  • Polyketides / metabolism

Substances

  • Bacterial Proteins
  • Polyketides