› 6nvu

X-ray diffraction
2.5Å resolution

Crystal structure of TLA-1 extended spectrum Beta-lactamase in complex with Clavulanic Acid

Released:
DOI: 10.2210/pdb6nvu/pdb
PDB entry 6nvu coloured by chain, front view.
PDB entry 6nvu coloured by chain, side view.
PDB entry 6nvu coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The crystal structure of ESBL TLA-1 in complex with clavulanic acid reveals a second acylation site.
Cifuentes-Castro V, Rodríguez-Almazán C, Silva-Sánchez J, Rudiño-Piñera E
Biochem Biophys Res Commun 522 545-551 (2020)
PMID: 31780261

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-194953 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 277 amino acids
Theoretical weight: 31.06 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9X6W1 (Residues: 36-312; Coverage: 99%)
Gene name: tla-1
Sequence domains: Beta-lactamase enzyme family

Ligands and Environments

7 bound ligands:
Ligand SO4 1 x SO4
Ligand ACT 3 x ACT
Ligand TEM 1 x TEM
Ligand CL 2 x CL
Ligand L4A 1 x L4A
Ligand NA 1 x NA
Ligand J01 2 x J01
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P41212
Unit cell:
a: 98.64Å b: 98.64Å c: 100.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.201 0.266
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Extended Spectrum Beta-Lactamase (ESBL) Produced by Gram-Negative Bacteria in Trinidad and Tobago.
Akpaka et al. (2021)

2 mentions without citation

The role of adjuvants in overcoming antibacterial resistance due to enzymatic drug modification.
El-Khoury et al. (2022)
1 more