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

SASDWW3 – crTPpart2 of cysteine synthase A (CysK)

crTPpart2 of cysteine synthase A (CysK)
MWexperimental 14 kDa
MWexpected 16 kDa
VPorod 28 nm3
log I(s) 8.93×10-3 8.93×10-4 8.93×10-5 8.93×10-6
crTPpart2 of cysteine synthase A (CysK) small angle scattering data  s, nm-1
ln I(s)
crTPpart2 of cysteine synthase A (CysK) Guinier plot ln 8.93×10-3 Rg: 1.7 nm 0 (1.7 nm)-2 s2
(sRg)2I(s)/I(0)
crTPpart2 of cysteine synthase A (CysK) Kratky plot 1.104 0 3 sRg
p(r)
crTPpart2 of cysteine synthase A (CysK) pair distance distribution function Rg: 1.7 nm 0 Dmax: 6.2 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of crTPpart2 of CysK in 20 mM HEPES, 300 mM NaCl, pH 8 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.7 and 10.6 mg/ml were measured at 10°C. 40 successive 0.095 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. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.

crTPpart2 of cysteine synthase A (CysK) (crTPpart2_CysK)
Mol. type   Protein
Organism   Paulinella chromatophora
Olig. state   Monomer
Mon. MW   15.8 kDa
Sequence   FASTA