Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle.

Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K, Nature 568(7753):571-575 (2019) Europe PMC

SASDE36 – Human ATP-citrate synthase (ACLY) in HBS

ATP-citrate synthase

MW^experimental	480	kDa
MW^expected	458	kDa
V^Porod	738	nm³

log I(s) 1.54×10⁴ 1.54×10³ 1.54×10² 1.54×10¹

ATP-citrate synthase small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 1.55×10⁴ R_g: 6.0 nm 0 (6.0 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

p(r)	R_g: 6.1 nm 0 D_max: 17.5 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.5

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0
1.872

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Synchrotron SAXS data from solutions of ATP-citrate synthase (ACLY) in 20mM HEPES, 150mM NaCl, pH 7.2 were collected on the EMBL P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.124 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Size-exclusion chromatography SAXS (SEC-SAXS) was employed using a sample injection concentration of 24.00 mg/ml. Data were measured at through the SEC elution at 20°C. 900 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of an appropriate solvent-blank was subtracted using the CHROMIXS SEC-SAXS analysis package.

For two-state model displayed above, the weights of the respective states are 58% (top) and 42% (bottom).

ATP-citrate synthase
Mol. type		Protein
Organism		Homo sapiens
Olig. state		Tetramer
Mon. MW		114.6 kDa

UniProt		P53396-1
Sequence		FASTA