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 Feb)

doi: 10.1016/j.ijbiomac.2020.12.190 		Submitted to SASBDB: 2020 Nov 27
Published in SASBDB:

SASDKG4 – Malus domestica double bond reductase (MdDBR) apoform

Malus domestica double bond reductase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Malus domestica double bond reductase dimer, 77 kDa Malus domestica protein
Buffer: 50 mM Tris-HCl, 100 mM NaCl., pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2020 Oct 23
RgGuinier 3.0 nm
Dmax 9.9 nm
VolumePorod 110 nm3

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

Malus domestica double bond reductase experimental SAS data
PYMOL model
Sample: Malus domestica double bond reductase dimer, 77 kDa Malus domestica protein
Buffer: 50 mM Tris-HCl, 100 mM NaCl, 5 mM NADPH, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2020 Oct 23
RgGuinier 3.1 nm
Dmax 10.7 nm
VolumePorod 99 nm3