2MLH

NMR Solution Structure of Opa60 from N. Gonorrhoeae in FC-12 Micelles

2MLH の概要

• エントリーDOI: 10.2210/pdb2mlh/pdb
• 関連するPDBエントリー: 2maf
• NMR情報: BMRB: 19343
• 分子名称: Opacity protein opA60 (1 entity in total)
• 機能のキーワード: membrane protein, beta-barrel
• 由来する生物種: Neisseria gonorrhoeae
• 細胞内の位置: Cell outer membrane: Q04884
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27115.07

構造登録者

Fox, D.A.,Larsson, P.,Lo, R.H.,Kroncke, B.M.,Kasson, P.M.,Columbus, L. (登録日: 2014-02-27, 公開日: 2014-06-25, 最終更新日: 2024-05-15)

主引用文献

Fox, D.A.,Larsson, P.,Lo, R.H.,Kroncke, B.M.,Kasson, P.M.,Columbus, L.
Structure of the neisserial outer membrane protein opa60: loop flexibility essential to receptor recognition and bacterial engulfment.
J.Am.Chem.Soc., 136:9938-9946, 2014

PubMed Abstract: The structure and dynamics of Opa proteins, which we report herein, are responsible for the receptor-mediated engulfment of Neisseria gonorrheae or Neisseria meningitidis by human cells and can offer deep understanding into the molecular recognition of pathogen-host receptor interactions. Such interactions are vital to understanding bacterial pathogenesis as well as the mechanism of foreign body entry to a human cell, which may provide insights for the development of targeted pharmaceutical delivery systems. The size and dynamics of the extracellular loops of Opa60 required a hybrid refinement approach wherein membrane and distance restraints were used to generate an initial NMR structural ensemble, which was then further refined using molecular dynamics in a DMPC bilayer. The resulting ensemble revealed that the extracellular loops, which bind host receptors, occupy compact conformations, interact with each other weakly, and are dynamic on the nanosecond time scale. We predict that this conformational sampling is critical for enabling diverse Opa loop sequences to engage a common set of receptors.

PubMed: 24813921
DOI: 10.1021/ja503093y

実験手法

SOLUTION NMR