Hydroxyl radical footprinting modification reveals an intradomain communication pathway in EFL1 disrupted by a Shwachman-Diamond syndrome-associated mutation.

Zúñiga-Domínguez JA, Jain R, González-Andrade M, Farquhar ER, Chance MR, Gijsbers A, Sánchez-Puig N, Protein Sci 35(4):e70504 (2026) Europe PMC

SASDYF4 – Mutant Elongation Factor Like-1 protein

Mutated ribosome assembly protein 1 (R1086Q) with C-terminal tag (RSRSGSENLYFQGSHHHHHHHH)
MWexperimental 192 kDa
MWexpected 127 kDa
VPorod 314 nm3
log I(s) 3.99×10-2 3.99×10-3 3.99×10-4 3.99×10-5
Mutated ribosome assembly protein 1 (R1086Q) with C-terminal tag (RSRSGSENLYFQGSHHHHHHHH) small angle scattering data  s, nm-1
ln I(s)
Mutated ribosome assembly protein 1 (R1086Q) with C-terminal tag (RSRSGSENLYFQGSHHHHHHHH) Guinier plot ln 3.99×10-2 Rg: 4.7 nm 0 (4.7 nm)-2 s2
(sRg)2I(s)/I(0)
Mutated ribosome assembly protein 1 (R1086Q) with C-terminal tag (RSRSGSENLYFQGSHHHHHHHH) Kratky plot 1.104 0 √3 sRg
p(r)
Mutated ribosome assembly protein 1 (R1086Q) with C-terminal tag (RSRSGSENLYFQGSHHHHHHHH) pair distance distribution function Rg: 4.5 nm 0 Dmax: 15.2 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Mutant Elongation Factor Like-1 protein in 50 mM HEPES, 300 mM NaCl, 5 mM MgCl2, 5% glycerol, pH 8 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.095 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 6 mg/ml was injected at a 0.08 ml/min flow rate onto a Shodex KW403-4F column at 20°C. 600 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.

Mutated ribosome assembly protein 1 (R1086Q) with C-terminal tag (RSRSGSENLYFQGSHHHHHHHH) (EFL1 R1086Q)
Mol. type   Protein
Organism   Saccharomyces cerevisiae
Olig. state   Monomer
Mon. MW   127.1 kDa
 
UniProt   P53893 (1-1110)
Sequence   FASTA