Evidence for phospholipid export from the bacterial inner membrane by the Mla ABC transport system

Gareth Hughes, Stephen Hall, Claire Laxton, Pooja Sridhar, Amirul Mahadi, Caitlin Hatton, Thomas Piggot, Peter Wotherspoon, Aneika Leney, Douglas Ward, Mohammed Jamshad, Vaclav Spana, Ian Cadby, Christopher Harding, Georgia Isom, Jack Bryant, Rebecca Parr, Yasin Yakub, Mark Jeeves, Damon HuberIan Henderson, Luke Clifton, Andrew Lovering, Timothy Knowles

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The Mla pathway is believed to be involved in maintaining the asymmetrical Gram-negative outer membrane via retrograde phospholipid transport. The pathway is composed of 3 components: the outer membrane MlaA-OmpC/F complex, a soluble periplasmic protein, MlaC, and the inner membrane ATPase, MlaFEDB complex. Here we solve the crystal structure of MlaC in its phospholipid free closed apo conformation, revealing a pivoting β-sheet mechanism which functions to open and close the phospholipid-binding pocket. Using the apo form of MlaC we provide evidence that the inner membrane MlaFEDB machinery exports phospholipids to MlaC in the periplasm. Furthermore we confirm that the phospholipid export process occurs through the MlaD component of the MlaFEDB complex and that this process is independent of ATP. Our data provides evidence of an apparatus for lipid export away from the inner membrane and suggests that the Mla pathway may have a role in anterograde phospholipid transport.
Original languageEnglish
Pages (from-to)1692–1705
Number of pages14
JournalNature Microbiology
Issue number10
Early online date24 Jun 2019
Publication statusPublished - Oct 2019

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© 2019, The Author(s), under exclusive licence to Springer Nature Limited.


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