Tetracycline-modifying enzyme Sm TetX from Stenotrophomonas maltophilia

Malý M, Kolenko P, Stránský J, Švecová L, Dušková J, Koval' T, Skálová T, Trundová M, Adámková K, Černý J, Božíková P, Dohnálek J, Acta Crystallographica Section F Structural Biology Communications 79(7):180-192 (2023) DOI

SASDPV7 – FAD-dependent monooxygenase from Stenotrophomonas maltophilia (no reducing agent)

Monooxygenase (M154I, A283T)
MWexperimental 40 kDa
MWexpected 39 kDa
VPorod 59 nm3
log I(s) 1.34×10-1 1.34×10-2 1.34×10-3 1.34×10-4
Monooxygenase (M154I, A283T) small angle scattering data  s, nm-1
ln I(s)
Monooxygenase (M154I, A283T) Guinier plot ln 1.35×10-1 Rg: 2.4 nm 0 (2.4 nm)-2 s2
(sRg)2I(s)/I(0)
Monooxygenase (M154I, A283T) Kratky plot 1.104 0 √3 sRg
p(r)
Monooxygenase (M154I, A283T) pair distance distribution function Rg: 2.3 nm 0 Dmax: 6.8 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Monooxygenase (M154I, A283T) REFMAC model
log I(s)
 s, nm-1
Monooxygenase (M154I, A283T) DAMMIF model
SAXS data from solutions of FAD-dependent monooxygenase in 25 mM Bis-Tris, 150 mM NaCl, pH 6.5 were collected using an Anton Paar SAXSpoint 2.0 instrument at the Institute of Biotechnology, Czech Academy of Sciences / Centre of Molecular Structure (Vestec, Czech Republic) equipped with an Eiger R 1M detector at a sample-detector distance of 0.8 m and at a wavelength of λ = 0.134 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.40 mg/ml was measured at 4°C. 61 successive 15.600 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.

Monooxygenase (M154I, A283T)
Mol. type   Protein
Organism   Stenotrophomonas maltophilia
Olig. state   Monomer
Mon. MW   38.9 kDa
 
UniProt   A0A2Y9UCL1
Sequence   FASTA