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Architectures of lipid transport systems for the bacterial outer membrane

Damian C. Ekiert, Gira Bhabha, Garrett Greenan, Sergey Ovchinnikov, Jeffery S. Cox, Ronald D. Vale
doi: https://doi.org/10.1101/064360
Damian C. Ekiert
1 Department of Microbiology and Immunology, The University of California, San Francisco, 600 16th St, San Francisco, CA 94158, USA.
2 Department of Cellular and Molecular Pharmacology, The University of California, San Francisco, 600 16th St, San Francisco, CA 94158, USA.
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  • For correspondence: damian.ekiert@ucsf.edu
Gira Bhabha
2 Department of Cellular and Molecular Pharmacology, The University of California, San Francisco, 600 16th St, San Francisco, CA 94158, USA.
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Garrett Greenan
2 Department of Cellular and Molecular Pharmacology, The University of California, San Francisco, 600 16th St, San Francisco, CA 94158, USA.
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Sergey Ovchinnikov
3 Institute for Protein Design, University of Washington, Seattle, WA 98195, USA.
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Jeffery S. Cox
1 Department of Microbiology and Immunology, The University of California, San Francisco, 600 16th St, San Francisco, CA 94158, USA.
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Ronald D. Vale
2 Department of Cellular and Molecular Pharmacology, The University of California, San Francisco, 600 16th St, San Francisco, CA 94158, USA.
4 Howard Hughes Medical Institute, The University of California, San Francisco, 600 16th St, San Francisco, CA 94158, USA.
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SUMMARY

How phospholipids are trafficked between the bacterial inner and outer membranes through the intervening hydrophilic space of the periplasm is not known. Here we report that members of the mammalian cell entry (MCE) protein family form structurally diverse hexameric rings and barrels with a central channel capable of mediating lipid transport. The E. coli MCE protein, MlaD, forms a ring as part of a larger ABC transporter complex in the inner membrane, and employs a soluble lipid-binding protein to ferry lipids between MlaD and an outer membrane protein complex. In contrast, EM structures of two other E. coli MCE proteins show that YebT forms an elongated tube consisting of seven stacked MCE rings, and PqiB adopts a syringe-like architecture. Both YebT and PqiB create channels of sufficient length to span the entire periplasmic space. This work reveals diverse architectures of highly conserved protein-based channels implicated in the transport of lipids between the inner and outer membranes of bacteria and some eukaryotic organelles.

HIGHLIGHTS

  1. MCE proteins adopt diverse architectures for transporting lipids across the bacterial periplasm

  2. Cryo-EM and X-ray structures reveal how the MlaFEDB complex, along with MlaC, might shuttle lipids across the periplasm

  3. 3.9 Å cryo-EM structure of PqiB reveals a syringe-like architecture with a continuous central channel

  4. YebT forms a a segmented tube-like structure, and YebT and PqiB are poised to directly link the inner and outer membranes to facilitate lipid transport.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted October 01, 2016.
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Architectures of lipid transport systems for the bacterial outer membrane
Damian C. Ekiert, Gira Bhabha, Garrett Greenan, Sergey Ovchinnikov, Jeffery S. Cox, Ronald D. Vale
bioRxiv 064360; doi: https://doi.org/10.1101/064360
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Architectures of lipid transport systems for the bacterial outer membrane
Damian C. Ekiert, Gira Bhabha, Garrett Greenan, Sergey Ovchinnikov, Jeffery S. Cox, Ronald D. Vale
bioRxiv 064360; doi: https://doi.org/10.1101/064360

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