The molecular dissection of TRIM25's RNA-binding mechanism provides key insights into its antiviral activity.

Álvarez L, Haubrich K, Iselin L, Gillioz L, Ruscica V, Lapouge K, Augsten S, Huppertz I, Choudhury NR, Simon B, Masiewicz P, Lethier M, Cusack S, Rittinger K, Gabel F, Leitner A, Michlewski G, Hentze MW, Allain FHT, Castello A, Hennig J, Nat Commun 15(1):8485 (2024) Europe PMC

SASDK78 – E3 ubiquitin/ISG15 ligase TRIM25, apo form (TRIM25 apo)

E3 ubiquitin/ISG15 ligase TRIM25
MWexperimental 105 kDa
MWexpected 100 kDa
log I(s) 1.50×102 1.50×101 1.50×100 1.50×10-1
E3 ubiquitin/ISG15 ligase TRIM25 small angle scattering data  s, nm-1
ln I(s)
E3 ubiquitin/ISG15 ligase TRIM25 Guinier plot ln 1.51×102 Rg: 6.8 nm 0 (6.8 nm)-2 s2
(sRg)2I(s)/I(0)
E3 ubiquitin/ISG15 ligase TRIM25 Kratky plot 1.104 0 3 sRg
p(r)
E3 ubiquitin/ISG15 ligase TRIM25 pair distance distribution function Rg: 7.2 nm 0 Dmax: 30.2 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of TRIM25 apo in 20 mM MES, 75 mM NaCl, 1 mM TCEP, pH 6.5 were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.122 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.4 and 6 mg/ml were measured at 20°C. 20 successive 0.050 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

E3 ubiquitin/ISG15 ligase TRIM25 (TRIM25)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   50.1 kDa
 
UniProt   Q14258 (189-630)
Sequence   FASTA