The Paulinella chromatophore transit peptide part2 adopts a structural fold similar to the γ-glutamyl-cyclotransferase fold

Klimenko V, Reiners J, Applegate V, Reimann K, Popowicz G, Hoeppner A, Papadopoulos A, Smits S, Nowack E, Plant Physiology (2025) DOI

SASDWU3 – RNA helicase (RnaH)

RNA helicase (RnaH)
MWexperimental 64 kDa
MWexpected 63 kDa
VPorod 132 nm3
log I(s) 4.54×10-2 4.54×10-3 4.54×10-4 4.54×10-5
RNA helicase (RnaH) small angle scattering data  s, nm-1
ln I(s)
RNA helicase (RnaH) Guinier plot ln 4.54×10-2 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
RNA helicase (RnaH) Kratky plot 1.104 0 √3 sRg
p(r)
RNA helicase (RnaH) pair distance distribution function Rg: 3.8 nm 0 Dmax: 13.7 nm

Data validation

Fits and models

log I(s)
 s, nm-1
RNA helicase (RnaH) Rg histogram Rg, nm
RNA helicase (RnaH) EOM/RANCH model
RNA helicase (RnaH) EOM/RANCH model
RNA helicase (RnaH) EOM/RANCH model
SAXS data from solutions of RnaH in 20 mM HEPES, 300 mM NaCl, pH 8 were collected on a Xenocs Xeuss 2.0 Q-Xoom instrument at the Center for Structural Studies, Heinrich-Heine-University (Düsseldorf, Germany) using a Pilatus3 R 300K detector at a sample-detector distance of 0.6 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.2 and 9 mg/ml were measured at 10°C. 18 successive 600 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.

RNA helicase (RnaH) (crTPpart2_RnaH +RnaH)
Mol. type   Protein
Organism   Paulinella chromatophora
Olig. state   Monomer
Mon. MW   63.5 kDa
Sequence   FASTA