Binding by calmodulin is coupled to transient unfolding of the third FF domain of Prp40A.

Díaz Casas A, Cordoba JJ, Ferrer BJ, Balakrishnan S, Wurm JE, Pastrana-Ríos B, Chazin WJ, Protein Sci 32(4):e4606 (2023) Europe PMC

SASDPW6 – FF3 domain of pre-mRNA-processing factor 40 homolog A (Prp40A)

Pre-mRNA-processing factor 40 homolog A
MWexperimental 10 kDa
MWexpected 9 kDa
VPorod 13 nm3
log I(s) 4.01×101 4.01×100 4.01×10-1 4.01×10-2
Pre-mRNA-processing factor 40 homolog A small angle scattering data  s, nm-1
ln I(s)
Pre-mRNA-processing factor 40 homolog A Guinier plot ln 4.02×101 Rg: 1.6 nm 0 (1.6 nm)-2 s2
(sRg)2I(s)/I(0)
Pre-mRNA-processing factor 40 homolog A Kratky plot 1.104 0 √3 sRg
p(r)
Pre-mRNA-processing factor 40 homolog A pair distance distribution function Rg: 1.7 nm 0 Dmax: 7.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Pre-mRNA-processing factor 40 homolog A OTHER model
Synchrotron SAXS data from solutions of the FF3 domain of pre-mRNA-processing factor 40 homolog A in 50 mM HEPES, 100 mM NaCl, 2 mM CaCl2, 1 mM TCEP, pH 7.4 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.103 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 8.00 mg/ml was measured at 25°C. 800 successive 3 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.

Pre-mRNA-processing factor 40 homolog A
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   9.5 kDa
 
UniProt   O75400 (516-592)
Sequence   FASTA