› 4m99

X-ray diffraction
2.6Å resolution

Acetyltransferase domain of PglB from Neisseria gonorrhoeae FA1090 in complex with acetyl coenzyme A

Released:
DOI: 10.2210/pdb4m99/pdb
PDB entry 4m99 coloured by chain, front view.
PDB entry 4m99 coloured by chain, side view.
PDB entry 4m99 coloured by chain, top view.
Source organism: Neisseria gonorrhoeae FA 1090
Primary publication:
Biochemical analysis and structure determination of bacterial acetyltransferases responsible for the biosynthesis of UDP-N,N'-diacetylbacillosamine.
Morrison MJ, Imperiali B
J Biol Chem 288 32248-32260 (2013)
PMID: 24064219

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177088 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylgalactosaminyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 208 amino acids
Theoretical weight: 21.03 KDa
Source organism: Neisseria gonorrhoeae FA 1090
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5FAE1 (Residues: 196-403; Coverage: 50%)
Gene name: NGO_0085
Sequence domains: PglD N-terminal domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ACO 3 x ACO
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P43212
Unit cell:
a: 97.66Å b: 97.66Å c: 173.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.202 0.227
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

The renaissance of bacillosamine and its derivatives: pathway characterization and implications in pathogenicity.
Morrison et al. (2014)
6 other articles

3 mentions without citation

Postembryonic screen for mutations affecting spine development in zebrafish.
Gray et al. (2021)
2 more