› 6v83

X-ray diffraction
1.8Å resolution

Crystal structure of CTX-M-14 E166A/P167S/D240G beta-lactamase in complex with ceftazidime-1

Released:
DOI: 10.2210/pdb6v83/pdb
PDB entry 6v83 coloured by chain, front view.
PDB entry 6v83 coloured by chain, side view.
PDB entry 6v83 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Antagonism between substitutions in β-lactamase explains a path not taken in the evolution of bacterial drug resistance.
Brown CA, Hu L, Sun Z, Patel MP, Singh S, Porter JR, Sankaran B, Prasad BVV, Bowman GR, Palzkill T
J Biol Chem 295 7376-7390 (2020)
PMID: 32299911

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192210 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 27.87 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9L5C7 (Residues: 29-291; Coverage: 100%)
Gene names: BKL28_004840, BKL28_005521, BXT93_06855, CR538_26855, CTX-M-14, E4K51_21070, EIA08_25160, ETN48_p0088, HL563_21800, HL563_23665, HLZ39_20540, HLZ39_26710, RCS101_P0028, RCS103_P0010, RCS30_P0082, RCS56_P0085, RCS60_P0031, RCS63_P0006, RCS65_P0008, RCS66_P0053, RCS68_P0054, SAMEA4362930_00013, SAMEA4363083_00099, SAMEA4370290_00046, beta-lactamase CTX-M-14, bla, bla CTX-M-14, bla-CTX-M-14a, blaCTX-M-14, blaCTX-M-14a, blaCTX-M-14b, blaCTX-M-14c, blaCTX-M-27b, blaUOE-2, blatoho-3, pCT_085, pHK01_011
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand CAZ 1 x CAZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P41212
Unit cell:
a: 42.357Å b: 42.357Å c: 262.692Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.171 0.207
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 citation in other articles

Natural variants modify Klebsiella pneumoniae carbapenemase (KPC) acyl-enzyme conformational dynamics to extend antibiotic resistance.
Tooke et al. (2021)
7 more

1 mention without citation

Antagonism between substitutions in β-lactamase explains a path not taken in the evolution of bacterial drug resistance.
Brown et al. (2020)