› 2wvl

X-ray diffraction
2.81Å resolution

Mannosyl-3-phosphoglycerate synthase from Thermus thermophilus HB27 in complex with GDP-alpha-D-Mannose and Mg(II)

Released:
DOI: 10.2210/pdb2wvl/pdb
PDB entry 2wvl coloured by chain, front view.
PDB entry 2wvl coloured by chain, side view.
PDB entry 2wvl coloured by chain, top view.
Source organism: Thermus thermophilus HB27
Primary publication:
Structural analysis of Thermus thermophilus HB27 mannosyl-3-phosphoglycerate synthase provides evidence for a second catalytic metal ion and new insight into the retaining mechanism of glycosyltransferases.
Gonçalves S, Borges N, Esteves AM, Victor BL, Soares CM, Santos H, Matias PM
J Biol Chem 285 17857-68 (2010)
PMID: 20356840

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180876 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mannosyl-3-phosphogylcerate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 391 amino acids
Theoretical weight: 43.65 KDa
Source organism: Thermus thermophilus HB27
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q72K30 (Residues: 1-391; Coverage: 100%)
Gene name: TT_C0588
Sequence domains: Mannosyl-3-phosphoglycerate synthase (osmo_MPGsynth)
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

3 bound ligands:
Ligand GDD 2 x GDD
Ligand MG 2 x MG
Ligand ZN 5 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P41212
Unit cell:
a: 113.456Å b: 113.456Å c: 195.982Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.173 0.234
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Diversity, biological roles and biosynthetic pathways for sugar-glycerate containing compatible solutes in bacteria and archaea.
Empadinhas et al. (2011)
3 more

4 mentions without citation

Deep evolutionary analysis reveals the design principles of fold A glycosyltransferases.
Taujale et al. (2020)
3 more