Cryo-EM structure of a protein nanopore reveals lipid acyl chains as integral components.

A 2.5-angstrom cryo-EM structure of the M2 mutant of Mycobacterium smegmatis porin MspA in a phospholipid nanodisc shows lipid acyl chains forming an ordered annulus around the pore.

• Why it matters: Nanopore technologies need clearer structural insight into how pore-forming proteins engage lipid membranes, beyond protein-only models that miss membrane-specific interactions.
• What they did: The authors solved a 2.5-angstrom cryo-electron microscopy structure of M2 MspA embedded in a phospholipid nanodisc and resolved densities for surrounding lipid acyl chains contacting the transmembrane barrel.
• The result: The resolved densities indicate a substantially more ordered annular lipid environment than expected for a heterogeneous, nonspecific interface, and the M2 mutations modulate pore polarity linked to ion selectivity and transport.

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