What is it about?

Mycobacterium tuberculosis is the causative agent of tuberculosis in humans. The bacterium coats itself a glycogen-like alpha-glucan to help evade an immune response. Rather than use the well-known classical biosynthetic pathway for glycogen biosynthesis, this pathogen uses a recently discovered alternative pathway. The alternative GlgE pathway uses a different building block to the classical pathway. We have solved the first structure of a carbohydrate-active enzyme enzyme, GlgM, that generates this alternative building block in mycobacteria. We now have greater understanding of how this enzyme works and how it compares with other similar enzymes.

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Why is it important?

Understanding how this pathogen generates its cloak will help inform strategies to treat patients with tuberculosis.


GlgM could be targeted in tandem with other enzymes of the pathway to block the production of the cloak. However, GlgE and GlgB are primary targets of the pathway because they lead to the accumulation of the building block, which is toxic to the bacterium at high levels. Antibiotics that target GlgE and GlgB would therefore be most effective when GlgM is fully functional.

Stephen Bornemann
The Sainsbury Laboratory

Read the Original

This page is a summary of: Structure of the Mycobacterium smegmatis α-maltose-1-phosphate synthase GlgM, Acta Crystallographica Section F Structural Biology Communications, April 2020, International Union of Crystallography,
DOI: 10.1107/s2053230x20004343.
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