› 6rb3

X-ray diffraction
2.3Å resolution

Structural basis for recognition and ring-cleavage of the Pseudomonas quinolone signal (PQS) by AqdC variant in complex with its substrate

Released:
DOI: 10.2210/pdb6rb3/pdb
PDB entry 6rb3 coloured by chain, front view.
PDB entry 6rb3 coloured by chain, side view.
PDB entry 6rb3 coloured by chain, top view.
Source organism: Mycobacteroides abscessus
Primary publication:
Structural basis for recognition and ring-cleavage of the Pseudomonas quinolone signal (PQS) by AqdC, a mycobacterial dioxygenase of the α/β-hydrolase fold family.
Wullich SC, Kobus S, Wienhold M, Hennecke U, Smits SHJ, Fetzner S
J Struct Biol 207 287-294 (2019)
PMID: 31228546

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109350 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-heptyl-3-hydroxy-4(1H)-quinolone dioxygenase Chains: A, B, E
Molecule details ›
Chains: A, B, E
Length: 269 amino acids
Theoretical weight: 29.75 KDa
Source organism: Mycobacteroides abscessus
Expression system: Escherichia coli
UniProt:
  • Canonical: B1MFK2 (Residues: 1-269; Coverage: 100%)
Gene names: MAB_0303, aqdC
Sequence domains: alpha/beta hydrolase fold

Ligands and Environments

1 bound ligand:
Ligand JWW 3 x JWW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P43212
Unit cell:
a: 96.644Å b: 96.644Å c: 190.138Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.195 0.246
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Intercellular communication and social behaviors in mycobacteria.
Boopathi et al. (2022)
4 other articles

1 mention without citation

Stabilizing AqdC, a Pseudomonas Quinolone Signal-Cleaving Dioxygenase from Mycobacteria, by FRESCO-Based Protein Engineering.
Wullich et al. (2021)