› 4opr

X-ray diffraction
1.45Å resolution

Crystal structure of stabilized TEM-1 beta-lactamase variant v.13 carrying G238S mutation

Released:
DOI: 10.2210/pdb4opr/pdb
PDB entry 4opr coloured by chain, front view.
PDB entry 4opr coloured by chain, side view.
PDB entry 4opr coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Negative Epistasis and Evolvability in TEM-1 β-Lactamase--The Thin Line between an Enzyme's Conformational Freedom and Disorder.
Dellus-Gur E, Elias M, Caselli E, Prati F, Salverda ML, de Visser JA, Fraser JS, Tawfik DS
J Mol Biol 427 2396-409 (2015)
PMID: 26004540

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-185161 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 28.8 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8KMX3 (Residues: 24-286; Coverage: 100%)
Gene name: bla-TEM-94
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

3 bound ligands:
Ligand CA 1 x CA
Ligand PG4 1 x PG4
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2
Unit cell:
a: 153.83Å b: 46.18Å c: 34.41Å
α: 90° β: 93.12° γ: 90°
R-values:
R R work R free
0.107 0.104 0.148
Expression system: Escherichia coli

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Citations

14 review citations

Epistasis in protein evolution.
Starr et al. (2016)
13 more

1 mention without citation

Negative Epistasis and Evolvability in TEM-1 β-Lactamase--The Thin Line between an Enzyme's Conformational Freedom and Disorder.
Dellus-Gur et al. (2015)