Structure of an endogenous mycobacterial MCE lipid transporter
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Abstract
To replicate inside macrophages and cause tuberculosis, Mycobacterium tuberculosis must scavenge a variety of nutrients from the host 1,2. The mammalian cell entry (MCE) proteins are important virulence factors in M. tuberculosis 1,3, where they are encoded by large gene clusters and have been implicated in the transport of fatty acids 4-7 and cholesterol 1,4,8 across the impermeable mycobacterial cell envelope. Very little is known about how cargos are transported across this barrier, and it remains unclear how the approximately ten proteins encoded by a mycobacterial mce gene cluster assemble to transport cargo across the cell envelope. Here we report the cryo-electron microscopy (cryo-EM) structure of the endogenous Mce1 lipid-import machine of Mycobacterium smegmatis-a non-pathogenic relative of M. tuberculosis. The structure reveals how the proteins of the Mce1 system assemble to form an elongated ABC transporter complex that is long enough to span the cell envelope. The Mce1 complex is dominated by a curved, needle-like domain that appears to be unrelated to previously described protein structures, and creates a protected hydrophobic pathway for lipid transport across the periplasm. Our structural data revealed the presence of a subunit of the Mce1 complex, which we identified using a combination of cryo-EM and AlphaFold2, and name LucB. Our data lead to a structural model for Mce1-mediated lipid import across the mycobacterial cell envelope.
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- Authors
- Chen, J., Fruhauf, A., Fan, C., Ponce, J., Ueberheide, B., Bhabha, G., & Ekiert, D. C.
- Affiliations
- New York University (US)
- NYU Langone Health (US)
- Corresponding author
- Bhabha, Gira
- Ekiert, Damian C.
- ORCID
- Venue
- Nature
- Published
- 2023-07-26
- Volume
- 620
- Issue
- 7973
- Pages
- 445-452
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC12817965
- OpenAlex
- W4385289080
- Cited by
- 69
- References
- 96
- Citations by year
- 2026: 19 · 2025: 22 · 2024: 13 · 2023: 14
- FWCI
- 14.08
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- Nature (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- Research Square (acceptedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed Central (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- U.S. Department of Energy (grid.436923.9, 436923.9)
- Oregon Health and Science University (436923, grid.436923.9, 436923.9)
- Memorial Sloan-Kettering Cancer Center
- National Institutes of Health (1s10od010582-01a1, PEW-00033055)
- School of Medicine, New York University (P30CA016087)
- Office of Science (grid.436923.9)
- NYU Grossman School of Medicine (P30CA016087)
- National Cancer Institute (1S10OD010582-01A1, NIH/NCI P30CA016087, P30CA016087)
- National Institute of General Medical Sciences (U24GM129547)
- National Institute of Allergy and Infectious Diseases (R01AI174646)
- Biological and Environmental Research (grid.436923.9)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- Mycobacterium smegmatis, Mycobacterium tuberculosis, ABC transporters, mycobacterial cell envelope, protein complex structure, cholesterol transport, fatty acid uptake
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