› 5b36

X-ray diffraction
2.15Å resolution

Crystal Structure of the O-Phosphoserine Sulfhydrylase from Aeropyrum pernix Complexed with Cysteine

Released:
DOI: 10.2210/pdb5b36/pdb
PDB entry 5b36 coloured by chain, front view.
PDB entry 5b36 coloured by chain, side view.
PDB entry 5b36 coloured by chain, top view.
Source organism: Aeropyrum pernix K1
Primary publication:
Role of F225 in O-phosphoserine sulfhydrylase from Aeropyrum pernix K1.
Takeda E, Kunimoto K, Kawai Y, Kataoka M, Ishikawa K, Nakamura T
Extremophiles 20 733-45 (2016)
PMID: 27377295

Function and Biology Details

Reactions catalysed: 
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate
L-serine + L-homocysteine = L-cystathionine + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195452 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein CysO Chains: A, B
Molecule details ›
Chains: A, B
Length: 389 amino acids
Theoretical weight: 42.03 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9YBL2 (Residues: 1-389; Coverage: 100%)
Gene names: APE_1586, cysO
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
2 bound ligands:
Ligand CYS 2 x CYS
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P43212
Unit cell:
a: 74.181Å b: 74.181Å c: 278.994Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.18 0.246
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Cysteine Biosynthesis in Campylobacter jejuni: Substrate Specificity of CysM and the Dualism of Sulfide.
Hitchcock et al. (2022)

1 mention without citation

Cross-strand disulfides in the hydrogen bonding site of antiparallel β-sheet (aCSDhs): Forbidden disulfides that are highly strained, easily broken.
Haworth et al. (2019)