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

SASDFB3 – Human ATP-citrate synthers (ACLY) full length in HBS + Citrate

ATP-citrate synthase
MWexperimental 510 kDa
MWexpected 458 kDa
VPorod 787 nm3
log I(s) 1.21×105 1.21×104 1.21×103 1.21×102
ATP-citrate synthase small angle scattering data  s, nm-1
ln I(s)
ATP-citrate synthase Guinier plot ln 1.21×105 Rg: 6.2 nm 0 (6.2 nm)-2 s2
(sRg)2I(s)/I(0)
ATP-citrate synthase Kratky plot 1.104 0 √3 sRg
p(r)
ATP-citrate synthase pair distance distribution function Rg: 6.1 nm 0 Dmax: 19 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Human ATP-citrate synthers (ACLY) in 20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, pH 7.2 were collected on the EMBL P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 2M 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 16.00 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