Cryo-EM structure of the <i>Mycobacterium smegmatis</i> MmpL5-AcpM complex
The emergence and spread of multidrug-resistant tuberculosis (TB) present enormous challenges to the global public health. The causative agent, <i>Mycobacterium tuberculosis</i>, has now infected more than one-third of the world's population. Here, we report the first structure of the mycobacterial membrane protein large 5 (MmpL5), an essential transporter for iron acquisition, bound with the meromycolate extension acyl carrier protein M (AcpM), indicating a plausible pathway for mycobactin translocation. Our studies will ultimately inform an era in structure-guided drug design to combat TB infection.
Authors
- Georgiana E. Purdy (ORCID: https://orcid.org/0000-0002-0739-6867)
- Zhemin Zhang (ORCID: https://orcid.org/0000-0003-4110-3164)
- Rakesh Maharjan (ORCID: https://orcid.org/0000-0003-2217-3191)
- Edward Yu (ORCID: https://orcid.org/0000-0001-5912-1227)
- Philip A. Klenotic (ORCID: https://orcid.org/0000-0001-8429-0145)
- William D. Gregor (ORCID: https://orcid.org/0009-0002-7722-614X)
Institutions
- Oregon Health & Science University (US)
- University School (US)
- Case Western Reserve University (US)
Publication Details
- Journal
- mBio
- Published
- 2024-10-31
- DOI
- https://doi.org/10.1128/mbio.03035-24
- Citations
- 13
- Primary Topic
- Tuberculosis Research and Epidemiology
- Type
- article
- Field-Weighted Citation Impact
- 5.06
Funders
- Case Western Reserve University
- National Institutes of Health