2MLH

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

Summary for 2MLH

• Entry DOI: 10.2210/pdb2mlh/pdb
• Related: 2maf
• NMR Information: BMRB: 19343
• Descriptor: Opacity protein opA60 (1 entity in total)
• Functional Keywords: membrane protein, beta-barrel
• Biological source: Neisseria gonorrhoeae
• Cellular location: Cell outer membrane: Q04884
• Total number of polymer chains: 1
• Total formula weight: 27115.07

Authors

Fox, D.A.,Larsson, P.,Lo, R.H.,Kroncke, B.M.,Kasson, P.M.,Columbus, L. (deposition date: 2014-02-27, release date: 2014-06-25, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

SOLUTION NMR