Robust structural, kinetic and biophysical characterization of wild-type human ACOD1, selected mutants and their interaction with citraconate

Runge B, Oktay H, Fucci I, Merten E, Tarasov S, Fan L, Monteiro D, Journal of Structural Biology: X :100157 (2026) DOI

SASD2A2 – Cis-aconitate decarboxylase ACOD1 ACOD1 Arg273Ser mutant

cis-aconitate decarboxylase 1
MWexperimental 98 kDa
MWexpected 101 kDa
log I(s) 3.86×10-2 3.86×10-3 3.86×10-4 3.86×10-5
cis-aconitate decarboxylase 1 small angle scattering data  s, nm-1
ln I(s)
cis-aconitate decarboxylase 1 Guinier plot ln 3.86×10-2 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
cis-aconitate decarboxylase 1 Kratky plot 1.104 0 3 sRg

Data validation


Fits and models


log I(s)
 s, nm-1
cis-aconitate decarboxylase 1 OTHER model

Synchrotron SAXS data from solutions of Cis-aconitate decarboxylase ACOD1 ACOD1 Arg273Ser mutant in 20 mM HEPES , 150 mM NaCl, 0.5 mM TCEP, and 2% (v/v) glycerol, pH 7.5 were collected on the 12-ID-B beam line at the Advanced Photon Source (APS), Argonne National Laboratory storage ring (Lemont, IL, USA) using a Eiger2 S detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.0932 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 100.00 μl sample at 6.1 mg/ml was injected at a 0.30 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. 694 successive 0.300 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.

cis-aconitate decarboxylase 1 (ACOD1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   50.6 kDa
 
UniProt   A6NK06
Sequence   FASTA