One substrate many enzymes virtual screening uncovers missing genes of carnitine biosynthesis in human and mouse.

Malatesta M, Fornasier E, Di Salvo ML, Tramonti A, Zangelmi E, Peracchi A, Secchi A, Polverini E, Giachin G, Battistutta R, Contestabile R, Percudani R, Nat Commun 15(1):3199 (2024) Europe PMC

SASDSU8 – Threonine aldolase 1 tetramer at neutral pH

L-threonine aldolase
MWexperimental 167 kDa
MWexpected 165 kDa
VPorod 209 nm3
log I(s) 2.10×101 2.10×100 2.10×10-1 2.10×10-2
L-threonine aldolase small angle scattering data  s, nm-1
ln I(s)
L-threonine aldolase Guinier plot ln 2.11×101 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
L-threonine aldolase Kratky plot 1.104 0 √3 sRg
p(r)
L-threonine aldolase pair distance distribution function Rg: 3.6 nm 0 Dmax: 10.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
L-threonine aldolase PHENIX model
Synchrotron SAXS data from solutions of L-threonine aldolase in 20 mM Tris, 150 mM NaCl, 1 mM EDTA, 1 mM DTT, pH 7.8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 250.00 μl sample at 5.5 mg/ml was injected at a 0.50 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 20°C. One 0.500 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

L-threonine aldolase (Tha1)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Tetramer
Mon. MW   41.4 kDa
 
UniProt   Q6XPS7 (41-400)
Sequence   FASTA