› 2y4j

X-ray diffraction
2.3Å resolution

MANNOSYLGLYCERATE SYNTHASE IN COMPLEX WITH LACTATE

Released:
DOI: 10.2210/pdb2y4j/pdb
PDB entry 2y4j coloured by chain, front view.
PDB entry 2y4j coloured by chain, side view.
PDB entry 2y4j coloured by chain, top view.
Source organism: Rhodothermus marinus
Primary publication:
Substrate and metal ion promiscuity in mannosylglycerate synthase.
Nielsen MM, Suits MD, Yang M, Barry CS, Martinez-Fleites C, Tailford LE, Flint JE, Dumon C, Davis BG, Gilbert HJ, Davies GJ
J Biol Chem 286 15155-64 (2011)
PMID: 21288903

Function and Biology Details

Reaction catalysed: 
GDP-alpha-D-mannose + D-glycerate = GDP + 2-O-(alpha-D-mannopyranosyl)-D-glycerate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193164 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mannosylglycerate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 382 amino acids
Theoretical weight: 44.71 KDa
Source organism: Rhodothermus marinus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9RFR0 (Residues: 1-382; Coverage: 96%)
Gene name: mgs
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

3 bound ligands:
Ligand LAC 2 x LAC
Ligand TRS 2 x TRS
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3221
Unit cell:
a: 148.975Å b: 148.975Å c: 154.973Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.198 0.222
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

The conformational plasticity of glycosyltransferases.
Albesa-Jové et al. (2016)
2 more

1 mention without citation

Substrate and metal ion promiscuity in mannosylglycerate synthase.
Nielsen et al. (2011)