Structural model of human dUTPase in complex with a novel proteinaceous inhibitor.

Nyíri K, Mertens HDT, Tihanyi B, Nagy GN, Kőhegyi B, Matejka J, Harris MJ, Szabó JE, Papp-Kádár V, Németh-Pongrácz V, Ozohanics O, Vékey K, Svergun DI, Borysik AJ, Vértessy BG, Sci Rep 8(1):4326 (2018) Europe PMC

SASDC67 – SaPIbov1 pathogenicity island repressor

SaPIbov1 pathogenicity island repressor
MWI(0) 45 kDa
MWexpected 64 kDa
VPorod 100 nm3
log I(s) 3.10×10-2 3.10×10-3 3.10×10-4 3.10×10-5
SaPIbov1 pathogenicity island repressor small angle scattering data  s, nm-1
ln I(s)
SaPIbov1 pathogenicity island repressor Guinier plot ln 3.10×10-2 Rg: 3.3 nm 0 (3.3 nm)-2 s2
(sRg)2I(s)/I(0)
SaPIbov1 pathogenicity island repressor Kratky plot 1.104 0 √3 sRg
p(r)
SaPIbov1 pathogenicity island repressor pair distance distribution function Rg: 3.2 nm 0 Dmax: 10.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
SaPIbov1 pathogenicity island repressor OTHER model
log I(s)
 s, nm-1
SaPIbov1 pathogenicity island repressor DAMMIF model
Synchrotron SAXS data from solutions of SaPIbov1 pathogenicity island repressor in 50 mM HEPES 300 mM NaCl 5 mM MgCl2, pH 7.5 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.2 and 0.9 mg/ml were measured at 10°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.

SaPIbov1 pathogenicity island repressor (Stl)
Mol. type   Protein
Organism   Staphylococcus aureus
Olig. state   Dimer
Mon. MW   32.0 kDa
 
UniProt   E2FZP6 (13-278)
Sequence   FASTA