Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex

Janssen B, Gomes L, Koning R, Svergun D, Koster A, Fritzinger D, Vogel C, Gros P, The EMBO Journal 28(16):2469-2478 (2009) DOI

SASDNV2 – The pro-convertase formed by human FB and cobra venom factor (CVF)

Cobra venom factor
MWexperimental 220 kDa
MWexpected 185 kDa
VPorod 384 nm3
log I(s) 7.44×102 7.44×101 7.44×100 7.44×10-1
Cobra venom factor small angle scattering data  s, nm-1
ln I(s)
Cobra venom factor Guinier plot ln 7.45×102 Rg: 4.6 nm 0 (4.6 nm)-2 s2
(sRg)2I(s)/I(0)
Cobra venom factor Kratky plot 1.104 0 √3 sRg
p(r)
Cobra venom factor pair distance distribution function Rg: 4.6 nm 0 Dmax: 15 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Cobra venom factor PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of The pro-convertase formed by human FB and cobra venom factor (CVF) in 10 mM Tris 5 mM MgCl2 10 mM NaCl, pH 7.4 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a Pilatus 500K detector 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 1 and 2 mg/ml were measured . Four 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. Sample detector distance = UNKNOWN

Tags: X33
Cobra venom factor
Mol. type   Protein
Organism   Naja kaouthia
Olig. state   Monomer
Mon. MW   184.5 kDa
 
UniProt   Q91132
Sequence   FASTA
 
PDB ID   3HRZ