› 4rx2

X-ray diffraction
2.32Å resolution

A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis

Released:
DOI: 10.2210/pdb4rx2/pdb
PDB entry 4rx2 coloured by chain, front view.
PDB entry 4rx2 coloured by chain, side view.
PDB entry 4rx2 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
A triple mutant in the Ω-loop of TEM-1 β-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis.
Stojanoski V, Chow DC, Hu L, Sankaran B, Gilbert HF, Prasad BV, Palzkill T
J Biol Chem 290 10382-94 (2015)
PMID: 25713062

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-158652 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase TEM Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 263 amino acids
Theoretical weight: 28.88 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P62593 (Residues: 24-286; Coverage: 100%)
Gene names: bla, blaT-3, blaT-4, blaT-5, blaT-6
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand SO4 8 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P1
Unit cell:
a: 60.32Å b: 83.3Å c: 95.92Å
α: 90.06° β: 89.97° γ: 90.02°
R-values:
R R work R free
0.237 0.235 0.268
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Structural and Mechanistic Basis for Extended-Spectrum Drug-Resistance Mutations in Altering the Specificity of TEM, CTX-M, and KPC β-lactamases.
Palzkill T. (2018)
1 more

1 mention without citation

A triple mutant in the Ω-loop of TEM-1 β-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis.
Stojanoski et al. (2015)