› 1ocx

X-ray diffraction
2.15Å resolution

E. coli maltose-O-acetyltransferase

Released:
DOI: 10.2210/pdb1ocx/pdb
PDB entry 1ocx coloured by chain, front view.
PDB entry 1ocx coloured by chain, side view.
PDB entry 1ocx coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The structure and specificity of Escherichia coli maltose acetyltransferase give new insight into the LacA family of acyltransferases.
Lo Leggio L, Dal Degan F, Poulsen P, Andersen SM, Larsen S
Biochemistry 42 5225-35 (2003)
PMID: 12731863

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + maltose = CoA + acetyl-maltose
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160204 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Maltose O-acetyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 182 amino acids
Theoretical weight: 19.99 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P77791 (Residues: 2-183; Coverage: 100%)
Gene names: JW0448, b0459, maa, ylaD
Sequence domains:
Structure domains: Hexapeptide repeat proteins

Ligands and Environments

1 bound ligand:
Ligand PBM 5 x PBM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2221
Unit cell:
a: 64.623Å b: 106.238Å c: 175.433Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.194 0.235
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Cells need safety valves.
Danchin A. (2009)
2 more

4 mentions without citation

Structural and kinetic characterizations of the polysialic acid O-acetyltransferase OatWY from Neisseria meningitidis.
Lee et al. (2009)
3 more