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

SASDE86 – C. limicola ATP-citrate lyase (ACL) in HBS + Citrate + Coenzyme-A

ATP-citrate lyase
MWexperimental 420 kDa
MWexpected 429 kDa
VPorod 791 nm3
log I(s) 1.10×105 1.10×104 1.10×103 1.10×102
ATP-citrate lyase small angle scattering data  s, nm-1
ln I(s)
ATP-citrate lyase Guinier plot ln 1.10×105 Rg: 5.7 nm 0 (5.7 nm)-2 s2
(sRg)2I(s)/I(0)
ATP-citrate lyase Kratky plot 1.104 0 √3 sRg
p(r)
ATP-citrate lyase pair distance distribution function Rg: 5.8 nm 0 Dmax: 17.5 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of C. limicola acetyl citrate lyase ACL 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 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 lyase (ACL)
Mol. type   Protein
Organism   Chlorobium limicola
Olig. state   Tetramer
Mon. MW   107.3 kDa
Sequence   FASTA