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==NMR Solution Structure of Opa60 from N. Gonorrhoeae in FC-12 Micelles==
<StructureSection load='2mlh' size='340' side='right'caption='[[2mlh]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mlh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MLH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlh OCA], [https://pdbe.org/2mlh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mlh RCSB], [https://www.ebi.ac.uk/pdbsum/2mlh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mlh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OPAH_NEIGO OPAH_NEIGO] Implicated in a number of adherence functions. OPA proteins are implicated in pathogenesis and are subject to phase variation.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

Structure of the Neisserial Outer Membrane Protein Opa: Loop Flexibility Essential to Receptor Recognition and Bacterial Engulfment.,Fox DA, Larsson P, Lo RH, Kroncke BM, Kasson PM, Columbus L J Am Chem Soc. 2014 May 19. PMID:24813921<ref>PMID:24813921</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mlh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Neisseria gonorrhoeae]]
[[Category: Columbus L]]
[[Category: Fox DA]]
[[Category: Kasson PM]]
[[Category: Kroncke BM]]
[[Category: Larsson P]]
[[Category: Lo RH]]