› 4afy

X-ray diffraction
2.01Å resolution

Crystal structure of the FimX EAL domain in complex with reaction product pGpG

Released:
DOI: 10.2210/pdb4afy/pdb
PDB entry 4afy coloured by chain, front view.
PDB entry 4afy coloured by chain, side view.
PDB entry 4afy coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of an EAL domain in complex with reaction product 5'-pGpG.
Robert-Paganin J, Nonin-Lecomte S, Réty S
PLoS One 7 e52424 (2012)
PMID: 23285035

Function and Biology Details

Reaction catalysed: 
Cyclic di-3',5'-guanylate + H(2)O = 5'-phosphoguanylyl(3'->5')guanosine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190965 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
FimX Chains: A, B
Molecule details ›
Chains: A, B
Length: 274 amino acids
Theoretical weight: 30.28 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9HUK6 (Residues: 439-691; Coverage: 37%)
Gene names: PA4959, fimX
Sequence domains: EAL domain
Structure domains: EAL domain
5'-R(*GP*GP)-3' Chains: C, D
Molecule details ›
Chains: C, D
Length: 2 nucleotides
Theoretical weight: 645 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand MG 3 x MG
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P43212
Unit cell:
a: 104.33Å b: 104.33Å c: 154.24Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.239
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

8 citation in other articles

Oligoribonuclease is the primary degradative enzyme for pGpG in Pseudomonas aeruginosa that is required for cyclic-di-GMP turnover.
Orr et al. (2015)
7 more

2 mentions without citation

Dimerisation induced formation of the active site and the identification of three metal sites in EAL-phosphodiesterases.
Bellini et al. (2017)
1 more