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Structural studies on Mycobacterium tuberculosis HddA enzyme using small angle X-ray scattering and dynamics

Sumita Karan1, Ankita Behl1, Amin Sagar2

  • 1Rm-403/440, Structural Biology Lab, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India.

International Journal of Biological Macromolecules
|January 7, 2021
PubMed
Summary

The Mycobacterium tuberculosis HddA enzyme is crucial for GDP-D-α-D-heptose biosynthesis. Structural and functional studies reveal its monomeric nature, ATPase activity, and enhanced stability upon substrate binding, offering therapeutic targets against tuberculosis.

Keywords:
ATPase assayCircular dichroismDynamics simulationHomology modelingMtbHddASAXS

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Drug Discovery

Background:

  • Mycobacterium tuberculosis HddA enzyme catalyzes a key step in GDP-D-α-D-heptose biosynthesis.
  • Understanding MtbHddA's structure and function is vital for developing new anti-tuberculosis therapies.

Purpose of the Study:

  • To elucidate the structural and functional characteristics of the MtbHddA enzyme.
  • To investigate the impact of substrate binding on MtbHddA stability and conformation.

Main Methods:

  • Enzyme purification and characterization (size exclusion chromatography, ATPase assay).
  • Structural analysis using Small-Angle X-ray Scattering (SAXS) and Circular Dichroism (CD) spectroscopy.
  • Computational modeling and molecular dynamics simulations.

Main Results:

  • MtbHddA was purified as a monomer with ATPase activity.
  • SAXS confirmed a globular monomeric structure; CD revealed significant alpha-helix content and a melting temperature (Tm) of ~47.5°C.
  • Ligand binding (ATP+Mg2+, Mannose) significantly enhanced MtbHddA's thermal stability.
  • Structural models indicated a GHMP sugar kinase fold with conserved substrate binding sites, and simulations showed stabilized active site conformations upon binding.

Conclusions:

  • MtbHddA exhibits a stable, monomeric structure and ATPase activity.
  • Substrate binding enhances MtbHddA stability, suggesting a functional role for these interactions.
  • MtbHddA represents a promising therapeutic target for combating Mycobacterium tuberculosis infections.