The BRCT domain enhances DNA binding and catalytic efficiency of fungal PARPs.

Bainbridge AG Gianga TM, Hussain R, Parkin C, Longhurst AD, Helmstetter N, Farrer RA, Catania S, Siligardi G, Rack JGM, Nat Commun 17(1) (2026) Europe PMC

SASDXE9 – poly(ADP-ribose)polymerase 1 (Af-PARP1) apo protein

Aspergillus fumigatus poly(ADP-ribose)polymerase 1
MWexperimental 80 kDa
MWexpected 74 kDa
VPorod 131 nm3
log I(s) 8.97×10-2 8.97×10-3 8.97×10-4 8.97×10-5
Aspergillus fumigatus poly(ADP-ribose)polymerase 1 small angle scattering data  s, nm-1
ln I(s)
Aspergillus fumigatus poly(ADP-ribose)polymerase 1 Guinier plot ln 8.97×10-2 Rg: 4.4 nm 0 (4.4 nm)-2 s2
(sRg)2I(s)/I(0)
Aspergillus fumigatus poly(ADP-ribose)polymerase 1 Kratky plot 1.104 0 3 sRg
p(r)
Aspergillus fumigatus poly(ADP-ribose)polymerase 1 pair distance distribution function Rg: 4.2 nm 0 Dmax: 13.7 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of poly(ADP-ribose)polymerase 1 (Af-PARP1) apo protein in 20 mM HEPES, 150 mM NaCl, 2 mM TCEP, 2.5% (v/v) Glycerol, pH 7.5 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.09464 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 7.43 mg/ml was measured at 15°C. 600 successive 3 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.

Aspergillus fumigatus poly(ADP-ribose)polymerase 1 (Af-PARP1)
Mol. type   Protein
Organism   Aspergillus fumigatus
Olig. state   Monomer
Mon. MW   74.3 kDa
Sequence   FASTA