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Instruments / Technical Area	Publication Details	Published	Actions
I04-Macromolecular Crystallography	Evidence for phospholipid export from the bacterial inner membrane by the Mla ABC transport system Gareth W. Hughes , Stephen C. L. Hall , Claire S. Laxton , Pooja Sridhar , Amirul H. Mahadi , Caitlin Hatton , Thomas J. Piggot , Peter J. Wotherspoon , Aneika C. Leney , Douglas G. Ward , Mohammed Jamshad , Vaclav Spana , Ian T. Cadby , Christopher Harding , Georgia L. Isom , Jack A. Bryant , Rebecca J. Parr , Yasin Yakub , Mark Jeeves , Damon Huber , Ian R. Henderson , Luke A. Clifton , Andrew L. Lovering , Timothy J. Knowles Nature Microbiology 106 DOI: 10.1038/s41564-019-0481-y Diamond Proposal Number(s): [14692] Show Abstract ▼ Abstract: 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 three 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 that 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 provide evidence of an apparatus for lipid export away from the inner membrane and suggest that the Mla pathway may have a role in anterograde phospholipid transport.	Jun 2019

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I04-Macromolecular Crystallography

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