Structural underpinnings of Ric8A function as a G-protein α-subunit chaperone and guanine-nucleotide exchange factor.

Srivastava D, Gakhar L, Artemyev NO, Nat Commun 10(1):3084 (2019) Europe PMC

SASDF75 – Resistance to inhibitors of cholinesterase 8 homolog A (Ric8a) amino acids 1-452

Resistance to inhibitors of cholinesterase 8 homolog A
MWexperimental 53 kDa
MWexpected 51 kDa
VPorod 70 nm3
log I(s) 2.04×10-3 2.04×10-4 2.04×10-5 2.04×10-6
Resistance to inhibitors of cholinesterase 8 homolog A small angle scattering data  s, nm-1
ln I(s)
Resistance to inhibitors of cholinesterase 8 homolog A Guinier plot ln 2.04×10-3 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
Resistance to inhibitors of cholinesterase 8 homolog A Kratky plot 1.104 0 √3 sRg
p(r)
Resistance to inhibitors of cholinesterase 8 homolog A pair distance distribution function Rg: 3.0 nm 0 Dmax: 11.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Resistance to inhibitors of cholinesterase 8 homolog A PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of Ric8a 1-452 in 20 mM Tris, 150 mM KCl, 5 % glycerol, 1 mM TCEP, pH 8 were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory (Lemont, IL, USA) using a Pilatus3 X 1M detector at a sample-detector distance of 3.5 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 10.00 mg/ml was measured at 25°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Number of frames = UNKNOWN. SEC column = UNKNOWN. Sample injection volume = UNKNOWN. Flow rate = UNKNOWN

Resistance to inhibitors of cholinesterase 8 homolog A (Ric8a)
Mol. type   Protein
Organism   Bos taurus
Olig. state   Monomer
Mon. MW   51.0 kDa
 
UniProt   Q5E9J8 (1-452)
Sequence   FASTA
 
PDB ID   6N85