› 4wku

X-ray diffraction
2Å resolution

n-Alkylboronic Acid Inhibitors Reveal Determinants of Ligand Specificity in the Quorum-Quenching and Siderophore Biosynthetic Enzyme PvdQ

Released:
DOI: 10.2210/pdb4wku/pdb
PDB entry 4wku coloured by chain, front view.
PDB entry 4wku coloured by chain, side view.
PDB entry 4wku coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
n-Alkylboronic acid inhibitors reveal determinants of ligand specificity in the quorum-quenching and siderophore biosynthetic enzyme PvdQ.
Clevenger KD, Wu R, Liu D, Fast W
Biochemistry 53 6679-86 (2014)
PMID: 25290020

Function and Biology Details

Reaction catalysed: 
An N-acyl-L-homoserine lactone + H(2)O = L-homoserine lactone + a carboxylate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191265 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Acyl-homoserine lactone acylase PvdQ subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 17.99 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9I194 (Residues: 28-192; Coverage: 22%)
Gene names: PA2385, pvdQ, qsc112
Structure domains: Penicillin Amidohydrolase, domain 1
Acyl-homoserine lactone acylase PvdQ subunit beta Chain: B
Molecule details ›
Chain: B
Length: 548 amino acids
Theoretical weight: 60.63 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9I194 (Residues: 217-762; Coverage: 74%)
Gene names: PA2385, pvdQ, qsc112
Sequence domains: Penicillin amidase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 16 x GOL
Ligand 3QJ 1 x 3QJ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: C2221
Unit cell:
a: 121.131Å b: 168.243Å c: 94.945Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.215
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The versatility of boron in biological target engagement.
Diaz et al. (2017)
2 more

1 mention without citation

Crystal Structure and Mutational Analysis of Isomalto-dextranase, a Member of Glycoside Hydrolase Family 27.
Okazawa et al. (2015)