6TVP

Structure of Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM

Summary for 6TVP

• Entry DOI: 10.2210/pdb6tvp/pdb
• Descriptor: Alpha-maltose-1-phosphate synthase, SODIUM ION (3 entities in total)
• Functional Keywords: glgm, alpha-maltose-1-phosphate synthase, glycosyltransferase, carbohydrate-active enzymes., sugar binding protein
• Biological source: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
• Total number of polymer chains: 2
• Total formula weight: 87116.42

Authors

Syson, K.,Stevenson, C.E.M.,Lawson, D.M.,Bornemann, S. (deposition date: 2020-01-10, release date: 2020-04-22, Last modification date: 2024-05-15)

Primary citation

Syson, K.,Stevenson, C.E.M.,Lawson, D.M.,Bornemann, S.
Structure of the Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM.
Acta Crystallogr.,Sect.F, 76:175-181, 2020

PubMed Abstract: Mycobacterium tuberculosis produces glycogen (also known as α-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 α-maltose-1-phosphate rather than an NDP-glucose donor. One of the routes to α-maltose-1-phosphate is now known to involve the GlgA homologue GlgM, which uses ADP-glucose as a donor and α-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 Å 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.

PubMed: 32254051
DOI: 10.1107/S2053230X20004343

Experimental method

X-RAY DIFFRACTION (1.9 Å)