The catalytic core of an archaeal 2-oxoacid dehydrogenase multienzyme complex is a 42-mer protein assembly

Marrott N, Marshall J, Svergun D, Crennell S, Hough D, Danson M, van den Elsen J, FEBS Journal 279(5):713-723 (2012) DOI

SASDLG3 – Thermoplasma E2 catalytic core

Regulatory protein E2
MWexperimental 950 kDa
MWexpected 1037 kDa
VPorod 2473 nm3
log I(s) 1.88×103 1.88×102 1.88×101 1.88×100
Regulatory protein E2 small angle scattering data  s, nm-1
ln I(s)
Regulatory protein E2 Guinier plot ln 1.88×103 Rg: 8.8 nm 0 (8.8 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: 8.5 nm 0 Dmax: 22 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Regulatory protein E2 PDB (PROTEIN DATA BANK) model
log I(s)
 s, nm-1
Regulatory protein E2 DAMMIF model
Synchrotron SAXS data from solutions of 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 MAR 345 Image Plate 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 0.4 and 1.3 mg/ml were measured . Two successive 120 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 concentrations were extrapolated to infinite dilution and merged with the higher concentration 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   Other
Mon. MW   24.7 kDa
 
UniProt   P03120 (177-400)
Sequence   FASTA
 
PDB ID   4OFS