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

SASDE56 – Human ATP-citrate synthase (ACLY) in HBS + Citrate + Coenzyme-A

ATP-citrate synthase

MW^experimental	480	kDa
MW^expected	458	kDa
V^Porod	709	nm³

log I(s) 1.18×10⁴ 1.18×10³ 1.18×10² 1.18×10¹

ATP-citrate synthase small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 1.18×10⁴ R_g: 5.8 nm 0 (5.8 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

p(r)	R_g: 5.8 nm 0 D_max: 16.5 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.3

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0
1.504

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

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, 50mM Tris, 20mM citrate, 2mM coenzyme-A, 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.

SEC column = UNKNOWN. Sample injection volume = UNKNOWN. Flow rate = UNKNOWN

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

UniProt		P53396-1
Sequence		FASTA