› 4bd0

X-ray diffraction
1.21Å resolution

X-ray structure of a perdeuterated Toho-1 R274N R276N double mutant Beta-lactamase in complex with a fully deuterated boronic acid (BZB)

Released:
DOI: 10.2210/pdb4bd0/pdb
PDB entry 4bd0 coloured by chain, front view.
PDB entry 4bd0 coloured by chain, side view.
PDB entry 4bd0 coloured by chain, top view.
Source organism: Escherichia coli BL21
Primary publication:
Neutron and X-ray crystal structures of a perdeuterated enzyme inhibitor complex reveal the catalytic proton network of the Toho-1 β-lactamase for the acylation reaction.
Tomanicek SJ, Standaert RF, Weiss KL, Ostermann A, Schrader TE, Ng JD, Coates L
J Biol Chem 288 4715-22 (2013)
PMID: 23255594

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-175211 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Toho-1 Chain: A
Molecule details ›
Chain: A
Length: 261 amino acids
Theoretical weight: 28.1 KDa
Source organism: Escherichia coli BL21
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q47066 (Residues: 31-291; Coverage: 100%)
Gene name: bla
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
Ligand BZB 1 x BZB
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3221
Unit cell:
a: 72.5Å b: 72.5Å c: 97.67Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.118 0.117 0.133
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Neutron protein crystallography: A complementary tool for locating hydrogens in proteins.
O'Dell et al. (2016)
2 more

3 mentions without citation

One ring to rule them all: Current trends in combating bacterial resistance to the β-lactams.
King et al. (2016)
2 more