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

SASDM82 – Ubiquitin-fold modifier 1

Ubiquitin fold modifer 1
MWexperimental 7 kDa
MWexpected 9 kDa
VPorod 16 nm3
log I(s) 3.58×10-3 3.58×10-4 3.58×10-5 3.58×10-6
Ubiquitin fold modifer 1 small angle scattering data  s, nm-1
ln I(s)
Ubiquitin fold modifer 1 Guinier plot ln 3.59×10-3 Rg: 1.5 nm 0 (1.5 nm)-2 s2
(sRg)2I(s)/I(0)
Ubiquitin fold modifer 1 Kratky plot 1.104 0 √3 sRg
p(r)
Ubiquitin fold modifer 1 pair distance distribution function Rg: 1.4 nm 0 Dmax: 5.1 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Ubiquitin fold modifer 1 PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of Ubiquitin-fold modifier 1 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 (DESY; 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 1.56 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 fold modifer 1 (UFM1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   8.9 kDa
 
UniProt   P61960 (1-83)
Sequence   FASTA
 
PDB ID   1WXS