Structural insights into highly similar spatial organization of zinc-finger associated domains with a very low sequence similarity.

Bonchuk AN, Boyko KM, Nikolaeva AY, Burtseva AD, Popov VO, Georgiev PG, Structure (2022) Europe PMC

SASDMH3 – Zinc-finger associated domain of Drosophila Pita protein L45A

LD15650p (Pita, isoform A; L45A)
MWexperimental 32 kDa
MWexpected 26 kDa
VPorod 35 nm3
log I(s) 2.00×10-2 2.00×10-3 2.00×10-4 2.00×10-5
LD15650p (Pita, isoform A; L45A) small angle scattering data  s, nm-1
ln I(s)
LD15650p (Pita, isoform A; L45A) Guinier plot ln 2.01×10-2 Rg: 2.3 nm 0 (2.3 nm)-2 s2
(sRg)2I(s)/I(0)
LD15650p (Pita, isoform A; L45A) Kratky plot 1.104 0 √3 sRg
p(r)
LD15650p (Pita, isoform A; L45A) pair distance distribution function Rg: 2.4 nm 0 Dmax: 9.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
LD15650p (Pita, isoform A; L45A) OTHER model
Synchrotron SAXS data from solutions of the zinc-finger associated domain of Drosophila Pita protein (L45A) in 20 mM Tris, 100 mM NaCl, 5 mM DTT, pH 7.4 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 2.4 mg/ml were measured at 10°C. 60 successive 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.

Zinc-finger-associated domain from Pita protein bearing a L45A substitution.

LD15650p (Pita, isoform A; L45A) (Pita)
Mol. type   Protein
Organism   Drosophila melanogaster
Olig. state   Dimer
Mon. MW   13.0 kDa
 
UniProt   Q95RQ8 (1-111)
Sequence   FASTA