Mycobacterium tuberculosis produces glycogen (also known as alpha-glucan) to help evade human immunity. This pathogen uses the GlgE pathway to generate glycogen rather than the more well known glycogen synthase GlgA pathway, which is absent in this bacterium. Thus, the building block for this glucose polymer is alpha-maltose-1-phosphate rather than an NDP-glucose donor. One of the routes to alpha-maltose-1-phosphate is now known to involve the GlgA homologue GlgM, which uses ADP-glucose as a donor and alpha-glucose-1-phosphate as an acceptor. To help compare GlgA (a GT5 family member) with GlgM enzymes (GT4 family members), the X-ray crystal structure of GlgM from Mycobacterium smegmatis was solved to 1.9 angstrom resolution. While the enzymes shared a GT-B fold and several residues responsible for binding the donor substrate, they differed in some secondary-structural details, particularly in the N-terminal domain, which would be expected to be largely responsible for their different acceptor-substrate specificities.
|Number of pages||7|
|Journal||Acta crystallographica section f-Structural biology communications|
|Publication status||Published - 1 Apr 2020|
- alpha-maltose-1-phosphate synthase