Solution Structure Analysis Of An Exchange Protein Directly Activated By cAMP

Mark White.

SASDCR6 – Rap guanine nucleotide exchange factor 3 (isoform3) - binary form with cAMP

Rap guanine nucleotide exchange factor 3 (dimer)
MWI(0) 178 kDa
MWexpected 200 kDa
VPorod 415 nm3
log I(s) 1.97×100 1.97×10-1 1.97×10-2 1.97×10-3
Rap guanine nucleotide exchange factor 3 (dimer) small angle scattering data  s, nm-1
ln I(s)
Rap guanine nucleotide exchange factor 3 (dimer) Guinier plot ln 1.97×100 Rg: 5.3 nm 0 (5.3 nm)-2 s2
(sRg)2I(s)/I(0)
Rap guanine nucleotide exchange factor 3 (dimer) Kratky plot 1.104 0 3 sRg
p(r)
Rap guanine nucleotide exchange factor 3 (dimer) pair distance distribution function Rg: 5.2 nm 0 Dmax: 15.7 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Rap guanine nucleotide exchange factor 3 (dimer) CORAL model

log I(s)
 s, nm-1
Rap guanine nucleotide exchange factor 3 (dimer) DAMMIF model

SAXS data from solutions of Rap guanine nucleotide exchange factor 3 (isoform3) - binary form with cAMP - in 1mM EDTA, 10mM DTT, 500mM NaCl, 1mM cAMP, 10mM Tris, pH 9 were collected using a Rigaku BioSAXS-1000 instrument at the Sealy Center For Structural Biology, UTMB-G (Galveston, TX, USA) equipped with a Kratky-2D Rigaku BioSAXS-1000 detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.15418 nm (I(s) vs s, where s = 4πsin θ/λ and 2θ is the scattering angle). A sample concentration of 4 mg/ml was measured at 10°C. SAXS data were acquired from 4 successive 1800 second frames. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted to generate the data displayed for this entry.

Rap guanine nucleotide exchange factor 3 (dimer) (EPAC1B (dimer))
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   100.0 kDa
 
UniProt   O95398-3 (2-881)
Sequence   FASTA
 
PDB code   4ZF7