› 3fgp

X-ray diffraction
2.05Å resolution

2.05 a Crystal Structure of CysM from Mycobacterium Tuberculosis - Open and Closed Conformations

Released:
DOI: 10.2210/pdb3fgp/pdb
PDB entry 3fgp coloured by chain, front view.
PDB entry 3fgp coloured by chain, side view.
PDB entry 3fgp coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity.
Agren D, Schnell R, Schneider G
FEBS Lett 583 330-6 (2009)
PMID: 19101553

Function and Biology Details

Reaction catalysed: 
O-phospho-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH = [CysO sulfur-carrier protein]-Gly-NH-CH(2)-C(O)-S-L-cysteine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161926 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
O-phosphoserine sulfhydrylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 326 amino acids
Theoretical weight: 34.95 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WP53 (Residues: 1-323; Coverage: 100%)
Gene names: MTCY130.21, Rv1336, cysM
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 74.933Å b: 89.142Å c: 99.382Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.247
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Combatting antimicrobial resistance via the cysteine biosynthesis pathway in bacterial pathogens.
Hicks et al. (2022)
10 other articles