› 4wio

X-ray diffraction
3.15Å resolution

Crystal structure of the C89A GMP synthetase inactive mutant from Plasmodium falciparum in complex with glutamine

Released:
DOI: 10.2210/pdb4wio/pdb
PDB entry 4wio coloured by chain, front view.
PDB entry 4wio coloured by chain, side view.
PDB entry 4wio coloured by chain, top view.
Source organism: Plasmodium falciparum 3D7
Primary publication:
Active site coupling in Plasmodium falciparum GMP synthetase is triggered by domain rotation.
Ballut L, Violot S, Shivakumaraswamy S, Thota LP, Sathya M, Kunala J, Dijkstra BW, Terreux R, Haser R, Balaram H, Aghajari N
Nat Commun 6 8930 (2015)
PMID: 26592566

Function and Biology Details

Reaction catalysed: 
(1a) L-glutamine + H(2)O = L-glutamate + NH(4)(+)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184803 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GMP synthase [glutamine-hydrolyzing] Chain: A
Molecule details ›
Chain: A
Length: 567 amino acids
Theoretical weight: 65.31 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8IJR9 (Residues: 2-555; Coverage: 100%)
Gene names: GMPS, PF10_0123, PF3D7_1012600
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand GLN 1 x GLN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P43212
Unit cell:
a: 76.92Å b: 76.92Å c: 204.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.265 0.263 0.306
Expression system: Escherichia coli

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Citations

2 review citations

A structural perspective on the PP-loop ATP pyrophosphatase family.
Fellner et al. (2018)
1 more

3 mentions without citation

GMP Synthetase: Allostery, Structure, and Function.
Ballut et al. (2023)
2 more