› 4lmb

X-ray diffraction
1.91Å resolution

Crystal structure analysis of O-acetylserine sulfhydrylase CysK2 complexed with cystine from Microcystis aeruginosa 7806

Released:
DOI: 10.2210/pdb4lmb/pdb
PDB entry 4lmb coloured by chain, front view.
PDB entry 4lmb coloured by chain, side view.
PDB entry 4lmb coloured by chain, top view.
Source organism: Microcystis aeruginosa PCC 7806
Primary publication:
Structural and biochemical analyses of Microcystis aeruginosa O-acetylserine sulfhydrylases reveal a negative feedback regulation of cysteine biosynthesis.
Lu M, Xu BY, Zhou K, Cheng W, Jiang YL, Chen Y, Zhou CZ
Biochim Biophys Acta 1844 308-15 (2014)
PMID: 24275508

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-108813 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine synthase Chain: A
Molecule details ›
Chain: A
Length: 322 amino acids
Theoretical weight: 34.74 KDa
Source organism: Microcystis aeruginosa PCC 7806
Expression system: Escherichia coli
UniProt:
  • Canonical: A8YBP8 (Residues: 1-315; Coverage: 100%)
Gene name: IPF_3084
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P6522
Unit cell:
a: 99.846Å b: 99.846Å c: 164.141Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.202 0.23
Expression system: Escherichia coli

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Citations

1 review citation

Insights into multifaceted activities of CysK for therapeutic interventions.
Joshi et al. (2019)
2 other articles