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.
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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