Skip to Main content Skip to Navigation
Journal articles

Small-angle X-ray scattering- and nuclear magnetic resonance-derived conformational ensemble of the highly flexible antitoxin PaaA2.

Abstract : Antitoxins from prokaryotic type II toxin-antitoxin modules are characterized by a high degree of intrinsic disorder. The description of such highly flexible proteins is challenging because they cannot be represented by a single structure. Here, we present a combination of SAXS and NMR data to describe the conformational ensemble of the PaaA2 antitoxin from the human pathogen E. coli O157. The method encompasses the use of SAXS data to filter ensembles out of a pool of conformers generated by a custom NMR structure calculation protocol and the subsequent refinement by a block jackknife procedure. The final ensemble obtained through the method is validated by an established residual dipolar coupling analysis. We show that the conformational ensemble of PaaA2 is highly compact and that the protein exists in solution as two preformed helices, connected by a flexible linker, that probably act as molecular recognition elements for toxin inhibition.
Complete list of metadata

https://hal.univ-grenoble-alpes.fr/hal-01131143
Contributor : Frank Thomas Connect in order to contact the contributor
Submitted on : Friday, March 13, 2015 - 8:51:36 AM
Last modification on : Sunday, June 26, 2022 - 5:59:49 AM

Identifiers

  • HAL Id : hal-01131143, version 1
  • PUBMED : 24768114

Collections

Citation

Yann G J Sterckx, Alexander N Volkov, Wim F Vranken, Jaka Kragelj, Malene Ringkjøbing Jensen, et al.. Small-angle X-ray scattering- and nuclear magnetic resonance-derived conformational ensemble of the highly flexible antitoxin PaaA2.. Structure (London, England : 1993), 2014, 22 (6), pp.854-65. ⟨hal-01131143⟩

Share

Metrics

Record views

92