› 5k9g

X-ray diffraction
1.9Å resolution

Crystal Structure of GTP Cyclohydrolase-IB with Tris

Released:
DOI: 10.2210/pdb5k9g/pdb
PDB entry 5k9g coloured by chain, front view.
PDB entry 5k9g coloured by chain, side view.
PDB entry 5k9g coloured by chain, top view.
Source organism: Neisseria gonorrhoeae FA 1090
Primary publication:
Mechanism and catalytic strategy of the prokaryotic-specific GTP cyclohydrolase-IB.
Paranagama N, Bonnett SA, Alvarez J, Luthra A, Stec B, Gustafson A, Iwata-Reuyl D, Swairjo MA
Biochem J 474 1017-1039 (2017)
PMID: 28126741

Function and Biology Details

Reaction catalysed: 
GTP + H(2)O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177081 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTP cyclohydrolase FolE2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 257 amino acids
Theoretical weight: 28.81 KDa
Source organism: Neisseria gonorrhoeae FA 1090
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5F9K6 (Residues: 1-257; Coverage: 100%)
Gene names: NGO0387, folE2
Sequence domains: Type I GTP cyclohydrolase folE2
Structure domains: Urate Oxidase;

Ligands and Environments

4 bound ligands:
Ligand ZN 2 x ZN
Ligand EDO 8 x EDO
Ligand TRS 1 x TRS
Ligand FMT 1 x FMT
1 modified residue:
Ligand SNC 2 x SNC

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2221
Unit cell:
a: 92.707Å b: 100.557Å c: 114.017Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.221
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

Bacillus subtilis FolE is sustained by the ZagA zinc metallochaperone and the alarmone ZTP under conditions of zinc deficiency.
Chandrangsu et al. (2019)
8 more

2 mentions without citation

Mechanism and catalytic strategy of the prokaryotic-specific GTP cyclohydrolase-IB.
Paranagama et al. (2017)
1 more