› 6ioi

X-ray diffraction
1.6Å resolution

Crystal structure of Homoserine O-acetyltransferase in complex with CoA from Mycobacterium smegmatis ATCC 19420

Released:
DOI: 10.2210/pdb6ioi/pdb
PDB entry 6ioi coloured by chain, front view.
PDB entry 6ioi coloured by chain, side view.
PDB entry 6ioi coloured by chain, top view.
Source organism: Mycolicibacterium smegmatis
Primary publication:
Crystal structure and biochemical characterization of O-acetylhomoserine acetyltransferase from Mycobacterium smegmatis ATCC 19420.
Sagong HY, Hong J, Kim KJ
Biochem Biophys Res Commun 517 399-406 (2019)
PMID: 31378370

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106304 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Homoserine O-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 374 amino acids
Theoretical weight: 39.48 KDa
Source organism: Mycolicibacterium smegmatis
Expression system: Escherichia coli
UniProt:
  • Canonical: A0QSZ0 (Residues: 14-380; Coverage: 97%)
Gene names: MSMEG_1651, MSMEI_1613, metXA
Sequence domains: alpha/beta hydrolase fold

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: P212121
Unit cell:
a: 58.384Å b: 96.366Å c: 140.67Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.181 0.206
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Antifungal Effect of Penicillamine Due to the Selective Targeting of L-Homoserine O-Acetyltransferase.
Kuplińska et al. (2022)

1 mention without citation

Structural analysis of mycobacterial homoserine transacetylases central to methionine biosynthesis reveals druggable active site.
Chaton et al. (2019)