› 5eke

X-ray diffraction
3Å resolution

Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant)

Released:
DOI: 10.2210/pdb5eke/pdb
PDB entry 5eke coloured by chain, front view.
PDB entry 5eke coloured by chain, side view.
PDB entry 5eke coloured by chain, top view.
Source organism: Synechocystis sp. PCC 6803 substr. Kazusa
Primary publication:
Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis.
Ardiccioni C, Clarke OB, Tomasek D, Issa HA, von Alpen DC, Pond HL, Banerjee S, Rajashankar KR, Liu Q, Guan Z, Li C, Kloss B, Bruni R, Kloppmann E, Rost B, Manzini MC, Shapiro L, Mancia F
Nat Commun 7 10175 (2016)
PMID: 26729507

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176285 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uncharacterized glycosyltransferase sll0501 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 341 amino acids
Theoretical weight: 39.24 KDa
Source organism: Synechocystis sp. PCC 6803 substr. Kazusa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q55487 (Residues: 2-318; Coverage: 100%)
Gene name: sll0501
Sequence domains: Glycosyl transferase family 2

Ligands and Environments

2 bound ligands:
Ligand UDP 4 x UDP
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: C2
Unit cell:
a: 154.135Å b: 142.243Å c: 102.01Å
α: 90° β: 97.16° γ: 90°
R-values:
R R work R free
0.25 0.249 0.276
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Lipopolysaccharide O-antigens-bacterial glycans made to measure.
Whitfield et al. (2020)
7 more

3 mentions without citation

Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis.
Ardiccioni et al. (2016)
2 more