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Role of a PAS sensor domain in the Mycobacterium tuberculosis transcription regulator Rv1364c

Ravi Kumar Jaiswal1, G Manjeera, B Gopal

  • 1Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.

Biochemical and Biophysical Research Communications
|June 15, 2010
PubMed

Insights

The Mycobacterium tuberculosis regulator Rv1364c

Area of Science:

  • Molecular biology
  • Structural biology
  • Biochemistry

Background:

  • Rv1364c is a Mycobacterium tuberculosis transcriptional regulator controlling the stress response sigma factor sigma(F).
  • This protein possesses multiple domains, including a PAS domain, a phosphatase, a kinase, and an anti-anti-sigma factor domain.
  • Previous Small Angle X-ray Scattering (SAXS) data indicated Rv1364c exists as a homo-dimer in an elongated conformation.

Purpose of the Study:

  • To determine the crystal structure of the Rv1364c PAS domain.
  • To elucidate the structural basis for Rv1364c dimerization.
  • To investigate potential ligand-binding capabilities of the PAS domain.

Main Methods:

  • X-ray crystallography to determine the PAS domain structure.
  • Structural comparison with known PAS domains.

Main Results:

  • The crystal structure of the Rv1364c PAS domain was determined.
  • The structure provides a molecular basis for Rv1364c homo-dimerization.
  • The PAS domain exhibits features suggesting potential ligand binding.

Conclusions:

  • The Rv1364c PAS domain likely regulates anti-sigma activity through oligomerization.
  • Rv1364c function may be modulated by cellular signals or metabolic cues.
  • This structural insight contributes to understanding Mycobacterium tuberculosis gene regulation.

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