› 8ovh

X-ray diffraction
2.17Å resolution

Crystal structure of O-acetyl-L-homoserine sulfhydrolase from Saccharomyces cerevisiae in complex with Pyridoxal-5'-phosphate

Released:
DOI: 10.2210/pdb8ovh/pdb
Model geometry
Fit model/data
PDB entry 8ovh coloured by chain, front view.
PDB entry 8ovh coloured by chain, side view.
PDB entry 8ovh coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Enzymatic Synthesis of l-Methionine Analogues and Application in a Methyltransferase Catalysed Alkylation Cascade.
Mohr MKF, Saleem-Batcha R, Cornelissen NV, Andexer JN
Chemistry e202301503 (2023)
PMID: 37235813

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-218514 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Homocysteine/cysteine synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 464 amino acids
Theoretical weight: 50.9 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P06106 (Residues: 1-444; Coverage: 100%)
Gene names: L8003.1, MET15, MET17, MET25, YLR303W
Sequence domains: Cys/Met metabolism PLP-dependent enzyme

Ligands and Environments


Cofactor: Ligand PLP 4 x PLP
1 bound ligand:
Ligand PEG 4 x PEG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 61.579Å b: 118.218Å c: 131.381Å
α: 90° β: 92.908° γ: 90°
R-values:
R R work R free
0.175 0.172 0.238
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Methyltransferases from RiPP pathways: shaping the landscape of natural product chemistry.
Schröder et al. (2024)
1 other article