Solution structure and dynamics of the mitochondrial‐targeted GTPase ‐activating protein ( GAP ) VopE by an integrated NMR / SAXS approach

Smith K, Lee W, Tonelli M, Lee Y, Light S, Cornilescu G, Chakravarthy S, Protein Science (2022) DOI

SASDJV3 – GTPase-Activation Protein (GAP) domain (73-204) of Vibrio cholerae Outer Protein E (VopE)

Outer membrane virulence protein yopE
MWexperimental 15 kDa
MWexpected 15 kDa
VPorod 28 nm3
log I(s) 2.95×102 2.95×101 2.95×100 2.95×10-1
Outer membrane virulence protein yopE small angle scattering data  s, nm-1
ln I(s)
Outer membrane virulence protein yopE Guinier plot ln 2.96×102 Rg: 2.0 nm 0 (2.0 nm)-2 s2
(sRg)2I(s)/I(0)
Outer membrane virulence protein yopE Kratky plot 1.104 0 3 sRg
Dmax: 8 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the GAP domain of Vibrio cholerae Outer Protein E (VopE) in 10 mM HEPES-HCl, pH 7.4, 150 mM NaCl, 0.5 mM TCEP, were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory (Lemont, IL, USA) using a Pilatus3 X 1M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.1033 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 300 μl sample at 19.5 mg/ml was injected at a 0.75 ml/min flow rate onto a GE Superdex 75 Increase 10/300 column at 25°C. 1254 successive 1 second frames were collected through the entire SEC elution. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of an appropriate solvent-blank was subtracted from data acquired through the SEC elution peak of the sample.

UniParc reference: UPI0004E46228

Outer membrane virulence protein yopE (VopE)
Mol. type   Protein
Organism   Vibrio cholerae
Olig. state   Monomer
Mon. MW   14.9 kDa
 
UniProt   A0A655XAV0 (73-204)
Sequence   FASTA