High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE.

Azmi L, Bragginton EC, Cadby IT, Byron O, Roe AJ, Lovering AL, Gabrielsen M, Acta Crystallogr F Struct Biol Commun 76(Pt 9):414-421 (2020) Europe PMC

SASDC72 – Alcohol dehydrogenase from bifunctional alcohol/aldehyde dehydrogenase (P0A9Q8)

Aldehyde-alcohol dehydrogenase
MWexperimental 91 kDa
MWexpected 97 kDa
VPorod 146 nm3
log I(s) 6.10×10-2 6.10×10-3 6.10×10-4 6.10×10-5
Aldehyde-alcohol dehydrogenase small angle scattering data  s, nm-1
ln I(s)
Aldehyde-alcohol dehydrogenase Guinier plot ln 6.10×10-2 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Aldehyde-alcohol dehydrogenase Kratky plot 1.104 0 3 sRg
p(r)
Aldehyde-alcohol dehydrogenase pair distance distribution function Rg: 3.6 nm 0 Dmax: 16.9 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Aldehyde-alcohol dehydrogenase DAMMIF model
Aldehyde-alcohol dehydrogenase DAMFILT model

Synchrotron SAXS data, I(s) vs s (s = 4π sin θ/λ, where 2θ is the scattering angle and λ is the X-ray wavelength) were collected from a sample of alcohol dehydrogenase from a bifunctional alcohol/aldehyde dehydrogenase protein (P0A9Q8) using continuous-flow size-exclusion chromatography SAXS (SEC-SAXS) on the B21 beam line at the Diamond Light Source (Oxfordshire, UK). Data (131 successive 1 second frames) were collected using a Pilatus 2M detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.1 nm. The SEC mobile phase consisted of 20 mM Tris, 400 mM NaCl, 5% v/v glycerol, pH 7.5 (4°C) with a sample injection concentration of 10 mg/ml. Data obtained from solute-free eluates and SEC-elution peak were normalized to the intensity of the transmitted beam and radially averaged. The scattering of the solvent-blank was subtracted from the SEC-peak frames using ScÅtter and then analysed using Primus to produce the data displayed in this entry.

Aldehyde-alcohol dehydrogenase (AdhE)
Mol. type   Protein
Organism   Escherichia coli O157:H7
Olig. state   Dimer
Mon. MW   48.3 kDa
 
UniProt   P0A9Q8 (451-891)
Sequence   FASTA