Structural basis for specific RNA recognition by the alternative splicing factor RBM5.

Soni K, Jagtap PKA, Martínez-Lumbreras S, Bonnal S, Geerlof A, Stehle R, Simon B, Valcárcel J, Sattler M, Nat Commun 14(1):4233 (2023) Europe PMC

SASDM43 – RRM1-ZnF1 tandem domains of RNA-binding protein 5 (C191G mutant)

RNA-binding protein 5 (I107T, C191G)
MWexperimental 15 kDa
MWexpected 14 kDa
VPorod 28 nm3
log I(s) 1.08×101 1.08×100 1.08×10-1 1.08×10-2
RNA-binding protein 5 (I107T, C191G) small angle scattering data  s, nm-1
ln I(s)
RNA-binding protein 5 (I107T, C191G) Guinier plot ln 1.09×101 Rg: 1.7 nm 0 (1.7 nm)-2 s2
(sRg)2I(s)/I(0)
RNA-binding protein 5 (I107T, C191G) Kratky plot 1.104 0 √3 sRg
p(r)
RNA-binding protein 5 (I107T, C191G) pair distance distribution function Rg: 1.7 nm 0 Dmax: 5.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Synchrotron SAXS data from solutions of RRM1-ZnF1 tandem domains of RNA-binding protein 5 (C191G mutant) in 20 mM MES, 400 mM NaCl, 1 mM DTT, pH 6.5 were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector at a wavelength of λ = 0.09919 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.00 mg/ml was measured at 25°C. 15 successive 1 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.

Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN

RNA-binding protein 5 (I107T, C191G) (RBM5 (I107T, C191G))
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   13.9 kDa
 
UniProt   P52756 (94-210)
Sequence   FASTA