› 3jyi

X-ray diffraction
2.7Å resolution

Structural and biochemical evidence that a TEM-1 {beta}-lactamase Asn170Gly active site mutant acts via substrate-assisted catalysis

Released:
DOI: 10.2210/pdb3jyi/pdb
PDB entry 3jyi coloured by chain, front view.
PDB entry 3jyi coloured by chain, side view.
PDB entry 3jyi coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural and biochemical evidence that a TEM-1 beta-lactamase N170G active site mutant acts via substrate-assisted catalysis.
Brown NG, Shanker S, Prasad BV, Palzkill T
J Biol Chem 284 33703-12 (2009)
PMID: 19812041

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
Molecule details ›
Chains: A, B, C, D, E, F
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

2 bound ligands:
Ligand EPE 6 x EPE
Ligand PO4 4 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P43212
Unit cell:
a: 88.099Å b: 88.099Å c: 500.352Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.23 0.26
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Klebsiella pneumoniae Carbapenemase Variants Resistant to Ceftazidime-Avibactam: an Evolutionary Overview.
Hobson et al. (2022)
1 more

5 mentions without citation

Structural bioinformatic analysis of DsbA proteins and their pathogenicity associated substrates.
Santos-Martin et al. (2021)
4 more