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Related Concept Videos

Lipid Catabolism01:25

Lipid Catabolism

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Triglycerides serve as crucial long-term energy storage molecules in microorganisms, providing a dense source of metabolic energy. Their breakdown is mediated by lipases, which hydrolyze triglycerides into glycerol and free fatty acids. Each of these components follows distinct metabolic pathways, ultimately contributing to ATP synthesis and cellular energy homeostasis.Glycerol MetabolismGlycerol, released from triglyceride hydrolysis, is phosphorylated by glycerol kinase to form...
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Analysis of the Lipid Composition of Mycobacteria by Thin Layer Chromatography
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Structural basis for triacylglyceride extraction from mycobacterial inner membrane by MFS transporter Rv1410.

Sille Remm1, Dario De Vecchis2, Jendrik Schöppe3,4

  • 1Institute of Medical Microbiology, University of Zurich, Zürich, Switzerland.

Nature Communications
|October 13, 2023
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Summary

Mycobacterium tuberculosis uses transporter Rv1410 to move lipids that protect its cell envelope. Structural and simulation data reveal how this major facilitator superfamily (MFS) transporter extracts and channels lipids to LprG for mycomembrane sealing.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Mycobacterium tuberculosis possesses a unique, multi-layered hydrophobic cell envelope essential for its survival and resistance to antibiotics.
  • The Major Facilitator Superfamily (MFS) transporter Rv1410 and periplasmic lipoprotein LprG are implicated in the transport of triacylglycerides (TAGs), which are crucial for sealing the mycobacterial mycomembrane.

Purpose of the Study:

  • To elucidate the structural mechanism of a mycobacterial Rv1410 homologue involved in triacylglyceride transport.
  • To understand how Rv1410 interacts with LprG for the efficient sealing of the mycomembrane.

Main Methods:

  • X-ray crystallography to determine the 2.7 Å structure of the Rv1410 homologue.
  • Molecular Dynamics (MD) simulations and mutational analyses to investigate transporter function and lipid extraction pathways.

Main Results:

  • The determined structure revealed an outward-facing conformation with unique transmembrane helix extensions.
  • A small, hydrophobic cavity, constricted by an ion-lock, is proposed for lipid transport.
  • TAGs are likely extracted from the inner membrane via lateral clefts and channeled to LprG by the periplasmic helix extensions.

Conclusions:

  • The study provides a structural basis for Rv1410-mediated TAG transport, highlighting the role of its unique structural features.
  • The findings offer insights into the mechanism of mycomembrane biogenesis and potential targets for antitubercular therapies.