Molecular shape and prominent role of β-strand swapping in organization of dUTPase oligomers

Takács E, Barabás O, Petoukhov M, Svergun D, Vértessy B, FEBS Letters 583(5):865-871 (2009) DOI

SASDLX5 – Wild-type human mitochondrial deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase)

Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial
MWexperimental 50 kDa
MWexpected 80 kDa
VPorod 101 nm3
log I(s) 1.13×104 1.13×103 1.13×102 1.13×101
Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial small angle scattering data  s, nm-1
ln I(s)
Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial Guinier plot ln 1.13×104 Rg: 2.6 nm 0 (2.6 nm)-2 s2
(sRg)2I(s)/I(0)
Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial Kratky plot 1.104 0 √3 sRg
p(r)
Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial pair distance distribution function Rg: 2.5 nm 0 Dmax: 7 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial BUNCH model
Synchrotron SAXS data from solutions of dUTPase in 20 mM citrate, 1 mM DTT, 0.1 mM PMSF, 1 mM MgCl2, pH 5 were collected on the EMBL X33 beam line at DORIS III (DESY, Hamburg, Germany) using a MAR 345 Image Plate detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.40 mg/ml was measured. Two successive 60 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.

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN

Tags: X33
Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Trimer
Mon. MW   26.6 kDa
 
UniProt   P33316 (1-252)
Sequence   FASTA