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

  • Shuping Zheng
  • , Ying Zhou
  • , Joy Fleming
  • , Yafeng Zhou
  • , Mengting Zhang
  • , Shiliang Li
  • , Honglin Li
  • , Bingqi Sun
  • , Wei Liu*
  • , Lijun Bi
  • *Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

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.

Original languageEnglish
Pages (from-to)1445-1457
Number of pages13
JournalFEBS Letters
Volume592
Issue number8
DOIs
StatePublished - Apr 2018
Externally publishedYes

Keywords

  • MSMEG_0129
  • Mycobacterium tuberculosis
  • Rv0164
  • START domain superfamily
  • structure

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