6TVP

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

6TVP の概要

• エントリーDOI: 10.2210/pdb6tvp/pdb
• 分子名称: Alpha-maltose-1-phosphate synthase, SODIUM ION (3 entities in total)
• 機能のキーワード: glgm, alpha-maltose-1-phosphate synthase, glycosyltransferase, carbohydrate-active enzymes., sugar binding protein
• 由来する生物種: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87116.42

構造登録者

Syson, K.,Stevenson, C.E.M.,Lawson, D.M.,Bornemann, S. (登録日: 2020-01-10, 公開日: 2020-04-22, 最終更新日: 2024-05-15)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)