› 9b2j

X-ray diffraction
2.35Å resolution

Structure of the quorum quenching lactonase GcL I237M mutant

Released:
DOI: 10.2210/pdb9b2j/pdb
PDB entry 9b2j coloured by chain, front view.
PDB entry 9b2j coloured by chain, side view.
PDB entry 9b2j coloured by chain, top view.
Source organism: Parageobacillus caldoxylosilyticus
Primary publication:
Catalytic Redundancies and Conformational Plasticity Drives Selectivity and Promiscuity in Quorum Quenching Lactonases.
Corbella M, Bravo J, Demkiv AO, Calixto AR, Sompiyachoke K, Bergonzi C, Brownless AR, Elias MH, Kamerlin SCL
JACS Au 4 3519-3536 (2024)
PMID: 39328773

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100027 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 297 amino acids
Theoretical weight: 34.4 KDa
Source organism: Parageobacillus caldoxylosilyticus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A023DFE8 (Residues: 1-282; Coverage: 100%)
Gene name: GCA01S_030_00190
Sequence domains: Metallo-beta-lactamase superfamily

Ligands and Environments

5 bound ligands:
Ligand SO4 13 x SO4
Ligand CO 3 x CO
Ligand ACT 4 x ACT
Ligand EDO 7 x EDO
Ligand FE 3 x FE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: C2
Unit cell:
a: 147.4Å b: 110.3Å c: 79.4Å
α: 90° β: 115.9° γ: 90°
R-values:
R R work R free
0.185 0.184 0.199
Expression system: Escherichia coli BL21(DE3)

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