Structure and dynamics of UBA5-UFM1 complex formation showing new insights in the UBA5 activation mechanism

Fuchs S, Kikhney A, Schubert R, Kaiser C, Liebau E, Svergun D, Betzel C, Perbandt M, Journal of Structural Biology :107796 (2021) DOI

SASDGM6 – Ubiquitin activating enzyme 5 (1.9 mg/ml)

Ubiquitin-like modifier-activating enzyme 5
MWexperimental 47 kDa
MWexpected 68 kDa
VPorod 94 nm3
log I(s) 7.50×10-2 7.50×10-3 7.50×10-4 7.50×10-5
Ubiquitin-like modifier-activating enzyme 5 small angle scattering data  s, nm-1
ln I(s)
Ubiquitin-like modifier-activating enzyme 5 Guinier plot ln 7.50×10-2 Rg: 2.9 nm 0 (2.9 nm)-2 s2
(sRg)2I(s)/I(0)
Ubiquitin-like modifier-activating enzyme 5 Kratky plot 1.104 0 3 sRg
p(r)
Ubiquitin-like modifier-activating enzyme 5 pair distance distribution function Rg: 2.9 nm 0 Dmax: 9.8 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Ubiquitin-like modifier-activating enzyme 5 SASREF model
Ubiquitin-like modifier-activating enzyme 5 SASREF model
Ubiquitin-like modifier-activating enzyme 5 SASREF model

Synchrotron SAXS data from solutions of Ubiquitin activating enzyme 5 (1.9 mg/ml) in 20 mM Tris, 150 mM NaCl, 2 mM DTT, pH 7.5 were collected on the EMBL P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.123982 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.92 mg/ml was measured at 15°C. 50 successive 0.045 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.

Ubiquitin-like modifier-activating enzyme 5 (UBA5)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   34.2 kDa
 
UniProt   Q9GZZ9 (57-346)
Sequence   FASTA
 
PDB ID   5IAA