The patatin-like protein PlpD forms structurally dynamic homodimers in the Pseudomonas aeruginosa outer membrane

Sarah E. Hanson, Tyrone Dowdy, Mioara Larion, Matthew Thomas Doyle () and Harris D. Bernstein ()
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Sarah E. Hanson: National Institutes of Health
Tyrone Dowdy: National Institutes of Health
Mioara Larion: National Institutes of Health
Matthew Thomas Doyle: National Institutes of Health
Harris D. Bernstein: National Institutes of Health

Nature Communications, 2024, vol. 15, issue 1, 1-14

Abstract: Abstract Members of the Omp85 superfamily of outer membrane proteins (OMPs) found in Gram-negative bacteria, mitochondria and chloroplasts are characterized by a distinctive 16-stranded β-barrel transmembrane domain and at least one periplasmic POTRA domain. All previously studied Omp85 proteins promote critical OMP assembly and/or protein translocation reactions. Pseudomonas aeruginosa PlpD is the prototype of an Omp85 protein family that contains an N-terminal patatin-like (PL) domain that is thought to be translocated across the OM by a C-terminal β-barrel domain. Challenging the current dogma, we find that the PlpD PL-domain resides exclusively in the periplasm and, unlike previously studied Omp85 proteins, PlpD forms a homodimer. Remarkably, the PL-domain contains a segment that exhibits unprecedented dynamicity by undergoing transient strand-swapping with the neighboring β-barrel domain. Our results show that the Omp85 superfamily is more structurally diverse than currently believed and suggest that the Omp85 scaffold was utilized during evolution to generate novel functions.

Date: 2024
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DOI: 10.1038/s41467-024-48756-6

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