› 6tvp

X-ray diffraction
1.9Å resolution

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

Released:
DOI: 10.2210/pdb6tvp/pdb
PDB entry 6tvp coloured by chain, front view.
PDB entry 6tvp coloured by chain, side view.
PDB entry 6tvp coloured by chain, top view.
Source organism: Mycolicibacterium smegmatis MC2 155
Primary publication:
Structure of the Mycobacterium smegmatis α-maltose-1-phosphate synthase GlgM.
Syson K, Stevenson CEM, Lawson DM, Bornemann S
Acta Crystallogr F Struct Biol Commun 76 175-181 (2020)
PMID: 32254051

Function and Biology Details

Reaction catalysed: 
ADP-alpha-D-glucose + alpha-D-glucose-1-phosphate = ADP + alpha-maltose-1-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106431 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-maltose-1-phosphate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 401 amino acids
Theoretical weight: 43.54 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli
UniProt:
  • Canonical: A0R2E2 (Residues: 1-387; Coverage: 100%)
Gene names: MSMEG_5080, MSMEI_4954, glgA, glgM
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04, DIAMOND BEAMLINE I03
Spacegroup: P21212
Unit cell:
a: 135.371Å b: 144.928Å c: 46.468Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.212
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

A temperature-sensitive Mycobacterium smegmatis glgE mutation leads to a loss of GlgE enzyme activity and thermostability and the accumulation of α-maltose-1-phosphate.
Syson et al. (2021)
1 more

1 mention without citation

Structure of the Mycobacterium smegmatis α-maltose-1-phosphate synthase GlgM.
Syson et al. (2020)