› 2ft0

X-ray diffraction
1.66Å resolution

Crystal structure of TDP-fucosamine acetyltransferase (WecD)- complex with acetyl-CoA

Released:
DOI: 10.2210/pdb2ft0/pdb
PDB entry 2ft0 coloured by chain, front view.
PDB entry 2ft0 coloured by chain, side view.
PDB entry 2ft0 coloured by chain, top view.
Source organism: Escherichia coli CFT073
Primary publication:
Crystal structure of TDP-fucosamine acetyltransferase (WecD) from Escherichia coli, an enzyme required for enterobacterial common antigen synthesis.
Hung MN, Rangarajan E, Munger C, Nadeau G, Sulea T, Matte A
J Bacteriol 188 5606-17 (2006)
PMID: 16855251

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-galactose = CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-galactose
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-184446 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
dTDP-fucosamine acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 235 amino acids
Theoretical weight: 25.44 KDa
Source organism: Escherichia coli CFT073
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8FBQ3 (Residues: 2-224; Coverage: 100%)
Gene names: c4710, wecD
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand ACO 2 x ACO
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P43212
Unit cell:
a: 84.9Å b: 84.9Å c: 154.122Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.223
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress.
Hentchel et al. (2015)
5 more

3 mentions without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)
2 more