› 2q3d

X-ray diffraction
2.2Å resolution

2.2 A Resolution Crystal Structure of O-Acetylserine Sulfhydrylase (OASS) From MYCOBACTERIUM TUBERCULOSIS in Complex with the Reaction Intermediate ALPHA-AMINOACRYLATE

Released:
DOI: 10.2210/pdb2q3d/pdb
PDB entry 2q3d coloured by chain, front view.
PDB entry 2q3d coloured by chain, side view.
PDB entry 2q3d coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complex.
Schnell R, Oehlmann W, Singh M, Schneider G
J Biol Chem 282 23473-81 (2007)
PMID: 17567578

Function and Biology Details

Reaction catalysed: 
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161927 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
O-acetylserine sulfhydrylase Chain: A
Molecule details ›
Chain: A
Length: 313 amino acids
Theoretical weight: 33.07 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WP55 (Residues: 1-310; Coverage: 100%)
Gene names: MTCY98.03, Rv2334, cysK, cysK1
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
Ligand PDA 1 x PDA
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: P41212
Unit cell:
a: 71.785Å b: 71.785Å c: 181.179Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.249
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Expanding the enzyme universe: accessing non-natural reactions by mechanism-guided directed evolution.
Renata et al. (2015)
5 more

2 mentions without citation

Insights into multifaceted activities of CysK for therapeutic interventions.
Joshi et al. (2019)
1 more