3ZBE

E. coli O157 ParE2-associated antitoxin 2 (PaaA2)

3ZBE の概要

• エントリーDOI: 10.2210/pdb3zbe/pdb
• NMR情報: BMRB: 18841
• 分子名称: PAAA2 (1 entity in total)
• 機能のキーワード: toxin-antitoxin, partially disordered protein, saxs/nmr
• 由来する生物種: ESCHERICHIA COLI O157\:H7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8473.46

構造登録者

Sterckx, Y.G.J.,Van Nuland, N.A.J.,Vranken, W.F.,Loris, R. (登録日: 2012-11-08, 公開日: 2014-01-15, 最終更新日: 2024-01-31)

主引用文献

Sterckx, Y.G.,Volkov, A.N.,Vranken, W.F.,Kragelj, J.,Jensen, M.R.,Buts, L.,Garcia-Pino, A.,Jove, T.,Van Melderen, L.,Blackledge, M.,Van Nuland, N.A.,Loris, R.
Small-Angle X-Ray Scattering- and Nuclear Magnetic Resonance-Derived Conformational Ensemble of the Highly Flexible Antitoxin Paaa2.
Structure, 22:854-, 2014

PubMed 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.

PubMed: 24768114
DOI: 10.1016/J.STR.2014.03.012

実験手法

SOLUTION NMR