› 2vps

X-ray diffraction
2.75Å resolution

Structure Of The Bifunctional Leishmania Major Trypanothione Synthetase-Amidase

Released:
DOI: 10.2210/pdb2vps/pdb
PDB entry 2vps coloured by chain, front view.
PDB entry 2vps coloured by chain, side view.
PDB entry 2vps coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
Leishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities.
Fyfe PK, Oza SL, Fairlamb AH, Hunter WN
J Biol Chem 283 17672-80 (2008)
PMID: 18420578

Function and Biology Details

Reaction catalysed: 
Glutathione + glutathionylspermidine + ATP = N(1),N(8)-bis(glutathionyl)spermidine + ADP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180719 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase C51 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 652 amino acids
Theoretical weight: 74.53 KDa
Source organism: Leishmania major
Expression system: Escherichia coli
UniProt:
  • Canonical: Q711P7 (Residues: 1-652; Coverage: 100%)
Gene names: LMJF_27_1870, TRYS, tryS
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CL 5 x CL
Ligand BR 2 x BR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 71.05Å b: 85.6Å c: 168.34Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.204 0.25
Expression system: Escherichia coli

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Citations

11 review citations

Leishmania-macrophage interactions: insights into the redox biology.
Van Assche et al. (2011)
10 more

6 mentions without citation

Polyamines in protozoan pathogens.
Phillips MA. (2018)
5 more