Why are the 2-oxoacid dehydrogenase complexes so large? Generation of an active trimeric complex

Marrott N, Marshall J, Svergun D, Crennell S, Hough D, van den Elsen J, Danson M, Biochemical Journal 463(3):405-412 (2014) DOI

SASDLH3 – Truncated Thermoplasma E2 catalytic core

Regulatory protein E2
MWI(0) 80 kDa
MWexpected 73 kDa
VPorod 149 nm3
log I(s) 6.68×101 6.68×100 6.68×10-1 6.68×10-2
Regulatory protein E2 small angle scattering data  s, nm-1
ln I(s)
Regulatory protein E2 Guinier plot ln 6.68×101 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
Regulatory protein E2 Kratky plot 1.104 0 √3 sRg
p(r)
Regulatory protein E2 pair distance distribution function Rg: 3.2 nm 0 Dmax: 11 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Regulatory protein E2 CUSTOM IN-HOUSE model
Regulatory protein E2 CUSTOM IN-HOUSE model
Synchrotron SAXS data from solutions of Truncated Thermoplasma E2 catalytic core in 50 mM Tris ⁄ HCl, pH 8.8, 100 mM NaCl, pH 8.8 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a Pilatus 1M-W detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 3.2 and 5.8 mg/ml were measured . Eight successive 30 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN

Tags: X33
Regulatory protein E2
Mol. type   Protein
Organism   Human papillomavirus type 16
Olig. state   Trimer
Mon. MW   24.3 kDa
 
UniProt   P03120 (182-400)
Sequence   FASTA