› 6pux

X-ray diffraction
1.9Å resolution

Homoserine transacetylase MetX from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb6pux/pdb
PDB entry 6pux coloured by chain, front view.
PDB entry 6pux coloured by chain, side view.
PDB entry 6pux coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Structural analysis of mycobacterial homoserine transacetylases central to methionine biosynthesis reveals druggable active site.
Chaton CT, Rodriguez ES, Reed RW, Li J, Kenner CW, Korotkov KV
Sci Rep 9 20267 (2019)
PMID: 31889085

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-161712 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Homoserine O-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 366 amino acids
Theoretical weight: 38.26 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WJY9 (Residues: 10-372; Coverage: 96%)
Gene names: MTV016.41, Rv3341, metA, metXA
Sequence domains: alpha/beta hydrolase fold

Ligands and Environments

4 bound ligands:
Ligand SO4 9 x SO4
Ligand MG 6 x MG
Ligand CL 3 x CL
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 47.46Å b: 86.68Å c: 208.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.202
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Molecular targets for antifungals in amino acid and protein biosynthetic pathways.
Kuplińska et al. (2021)
1 more

3 mentions without citation

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