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PDBsum entry 2mlh
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Membrane protein
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PDB id
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2mlh
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References listed in PDB file
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Key reference
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Title
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Structure of the neisserial outer membrane protein opa₆₀: loop flexibility essential to receptor recognition and bacterial engulfment.
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Authors
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D.A.Fox,
P.Larsson,
R.H.Lo,
B.M.Kroncke,
P.M.Kasson,
L.Columbus.
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Ref.
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J Am Chem Soc, 2014,
136,
9938-9946.
[DOI no: ]
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PubMed id
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Abstract
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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.
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