The biological assembly of OXA-48 reveals a dimer interface with high charge complementarity and very high affinity.

Lund BA, Thomassen AM, Nesheim BHB, Carlsen TJO, Isaksson J, Christopeit T, Leiros HS, FEBS J (2018) Europe PMC

SASDEM3 – Dimeric class D beta-lactamase OXA-48

Beta-lactamase
MWexperimental 50 kDa
MWexpected 56 kDa
VPorod 74 nm3
log I(s) 2.70×101 2.70×100 2.70×10-1 2.70×10-2
Beta-lactamase small angle scattering data  s, nm-1
ln I(s)
Beta-lactamase Guinier plot ln 2.70×101 Rg: 2.5 nm 0 (2.5 nm)-2 s2
(sRg)2I(s)/I(0)
Beta-lactamase Kratky plot 1.104 0 √3 sRg
p(r)
Beta-lactamase pair distance distribution function Rg: 2.5 nm 0 Dmax: 7.4 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Beta-lactamase PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of dimeric class D beta-lactamase (OXA-48) in 50 mM HEPES, 50 mM K2SO4, pH 7, were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Dectris Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.09919 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.1 and 13 mg/ml were measured at 25°C. 10 successive 10 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration(s) were merged with the higher concentration high angle data to yield the final composite scattering curve.

Beta-lactamase (OXA-48)
Mol. type   Protein
Organism   Klebsiella pneumoniae
Olig. state   Dimer
Mon. MW   28.2 kDa
 
UniProt   Q6XEC0 (22-265)
Sequence   FASTA
 
PDB ID   5DTK