The structural and functional characterization of Malus domestica double bond reductase MdDBR provides insights towards the identification of its substrates

Caliandro R, Polsinelli I, Demitri N, Musiani F, Martens S, Benini S, International Journal of Biological Macromolecules 171:89-99 (2021) DOI

SASDKH4 – Malus domestica double bond reductase in the presence of NADPH 5mM

Malus domestica double bond reductase
MWexperimental 91 kDa
MWexpected 77 kDa
VPorod 99 nm3
log I(s) 2.65×100 2.65×10-1 2.65×10-2 2.65×10-3
Malus domestica double bond reductase small angle scattering data  s, nm-1
ln I(s)
Malus domestica double bond reductase Guinier plot ln 2.65×100 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
Malus domestica double bond reductase Kratky plot 1.104 0 √3 sRg
p(r)
Malus domestica double bond reductase pair distance distribution function Rg: 3.2 nm 0 Dmax: 10.7 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Malus domestica double bond reductase PYMOL model
log I(s)
 s, nm-1
Malus domestica double bond reductase PYMOL model
log I(s)
 s, nm-1
Malus domestica double bond reductase PYMOL model
SAXS data from solutions of Malus domestica double bond reductase in 50 mM Tris-HCl, 100 mM NaCl, 5 mM NADPH, pH 7.5 were collected using an Anton Paar SAXSpoint 2.0 instrument equipped with a Eiger R 1M detector (Vestec, Czech Republic) 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 2.20 mg/ml was measured at 20°C. 30 successive 60 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.

Malus domestica double bond reductase (MdDBR)
Mol. type   Protein
Organism   Malus domestica
Olig. state   Dimer
Mon. MW   38.4 kDa
Sequence   FASTA
 
PDB ID   6YTZ