The Chlamydia pneumoniae effector SemD exploits its host’s endocytic machinery by structural and functional mimicry

Kocher F, Applegate V, Reiners J, Port A, Spona D, Hänsch S, Mirzaiebadizi A, Ahmadian M, Smits S, Hegemann J, Mölleken K, Nature Communications 15(1) (2024) DOI

SASDTR5 – BR-GBD (apo form of actin nucleation-promoting factor WASL)

Actin nucleation-promoting factor WASL
MWexperimental 19 kDa
MWexpected 19 kDa
VPorod 19 nm3
log I(s) 4.56×102 4.56×101 4.56×100 4.56×10-1
Actin nucleation-promoting factor WASL small angle scattering data  s, nm-1
ln I(s)
Actin nucleation-promoting factor WASL Guinier plot ln 4.56×102 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
Actin nucleation-promoting factor WASL Kratky plot 1.104 0 3 sRg
p(r)
Actin nucleation-promoting factor WASL pair distance distribution function Rg: 2.9 nm 0 Dmax: 9.9 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of BR-GBD in 137 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4, 3% glycerol, pH 8.5 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). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 100.00 μl sample at 10 mg/ml was injected at a 0.60 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 20°C. 2400 successive 0.995 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.

Actin nucleation-promoting factor WASL (BR-GBD)
Mol. type   Protein
Organism   Rattus norvegicus
Olig. state   Monomer
Mon. MW   19.5 kDa
 
UniProt   O08816 (141-273)
Sequence   FASTA