› 6apa

X-ray diffraction
1.86Å resolution

Crystal structure of TEM1 beta-lactamase mutant I263A

Released:
DOI: 10.2210/pdb6apa/pdb
PDB entry 6apa coloured by chain, front view.
PDB entry 6apa coloured by chain, side view.
PDB entry 6apa coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
A Structural Basis for 129 Xe Hyper-CEST Signal in TEM-1 β-Lactamase.
Roose BW, Zemerov SD, Wang Y, Kasimova MA, Carnevale V, Dmochowski IJ
Chemphyschem 20 260-267 (2019)
PMID: 30151973

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
Molecule details ›
Chains: A, B, C, D
Length: 263 amino acids
Theoretical weight: 28.87 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 60.669Å b: 84.292Å c: 95.914Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.213 0.249
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

Molecular Sensing with Host Systems for Hyperpolarized 129Xe.
Jayapaul et al. (2020)
2 more

1 mention without citation

Biotransformations catalyzed by multimeric enzymes: stabilization of tetrameric ampicillin acylase permits the optimization of ampicillin synthesis under dissociation conditions.
Fernández-Lafuente et al. (2001)