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

SASDXF9 – poly(ADP-ribose)polymerase 1 (Af-PARP1) with N-terminal dBRCT domain truncation

Aspergillus fumigatus poly(ADP-ribosyl)polymerase 1 dBRCT
MWexperimental 65 kDa
MWexpected 58 kDa
VPorod 111 nm3
log I(s) 2.17×10-2 2.17×10-3 2.17×10-4 2.17×10-5
Aspergillus fumigatus poly(ADP-ribosyl)polymerase 1 dBRCT small angle scattering data  s, nm-1
ln I(s)
Aspergillus fumigatus poly(ADP-ribosyl)polymerase 1 dBRCT Guinier plot ln 2.18×10-2 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Aspergillus fumigatus poly(ADP-ribosyl)polymerase 1 dBRCT Kratky plot 1.104 0 √3 sRg
p(r)
Aspergillus fumigatus poly(ADP-ribosyl)polymerase 1 dBRCT pair distance distribution function Rg: 3.3 nm 0 Dmax: 10.9 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of poly(ADP-ribose)polymerase 1 (Af-PARP1) with N-terminal dBRCT domain truncation 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 2.89 mg/ml was measured at 15°C. 630 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-ribosyl)polymerase 1 dBRCT (Af-PARP1 dBRCT)
Mol. type   Protein
Organism   Aspergillus fumigatus
Olig. state   Monomer
Mon. MW   57.8 kDa
Sequence   FASTA