› 2b61

X-ray diffraction
1.65Å resolution

Crystal Structure of Homoserine Transacetylase

Released:
DOI: 10.2210/pdb2b61/pdb
PDB entry 2b61 coloured by chain, front view.
PDB entry 2b61 coloured by chain, side view.
PDB entry 2b61 coloured by chain, top view.
Source organism: Haemophilus influenzae
Primary publication:
Crystal structure of homoserine transacetylase from Haemophilus influenzae reveals a new family of alpha/beta-hydrolases.
Mirza IA, Nazi I, Korczynska M, Wright GD, Berghuis AM
Biochemistry 44 15768-73 (2005)
PMID: 16313180

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155249 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Homoserine O-acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 377 amino acids
Theoretical weight: 42.54 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
  • Canonical: P45131 (Residues: 1-358; Coverage: 100%)
Gene names: HI_1263, met2, metXA
Sequence domains: alpha/beta hydrolase fold
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P3121
Unit cell:
a: 85.264Å b: 85.264Å c: 120.263Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 0.163 0.187
Expression system: Escherichia coli

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Citations

2 review citations

Amino acid biosynthesis: new architectures in allosteric enzymes.
Curien et al. (2008)
1 more

6 mentions without citation

Crystallographic study to determine the substrate specificity of an L-serine-acetylating enzyme found in the D-cycloserine biosynthetic pathway.
Oda et al. (2013)
5 more