Structural Organization and Dynamics of Homodimeric Cytohesin Family Arf GTPase Exchange Factors in Solution and on Membranes.

Das S, Malaby AW, Nawrotek A, Zhang W, Zeghouf M, Maslen S, Skehel M, Chakravarthy S, Irving TC, Bilsel O, Cherfils J, Lambright DG, Structure (2019) Europe PMC

SASDEV9 – Cytohesin-2; ARF nucleotide-binding site opener, ARNO truncation mutant

Cytohesin-2; ARNO truncation mutant
MWexperimental 42 kDa
MWexpected 40 kDa
VPorod 63 nm3
log I(s) 3.04×10-2 3.04×10-3 3.04×10-4 3.04×10-5
Cytohesin-2; ARNO truncation mutant small angle scattering data  s, nm-1
ln I(s)
Cytohesin-2; ARNO truncation mutant Guinier plot ln 3.04×10-2 Rg: 2.7 nm 0 (2.7 nm)-2 s2
Cytohesin-2; ARNO truncation mutant Kratky plot 1.104 0 3 sRg
Cytohesin-2; ARNO truncation mutant pair distance distribution function Rg: 2.8 nm 0 Dmax: 9.9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Cytohesin-2; ARNO truncation mutant DAMMIN model

Synchrotron SAXS data from solutions ofthe cytohesin-2; ARF nucleotide-binding site opener, ARNO truncation mutant in 300 mM NaCl, 2 mM 2-mercaptoethanol and 30 mM Tris-HCl, pH 7.5 were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a CCD AVIEX PCCD170170 detector at a sample-detector distance of 1.8 m and at a wavelength of λ = 0.1033 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 8.00 mg/ml was measured at 15°C. One 1.5 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Cytohesin-2; ARNO truncation mutant (ARNO-CC)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   39.9 kDa
UniProt   Q99418 (58-400)
Sequence   FASTA