Journal article
Structure-Function Profile of MmpL3, the Essential Mycolic Acid Transporter from Mycobacterium tuberculosis
JM Belardinelli, A Yazidi, L Yang, L Fabre, W Li, B Jacques, SK Angala, I Rouiller, HI Zgurskaya, J Sygusch, M Jackson
ACS Infectious Diseases | AMER CHEMICAL SOC | Published : 2016
Abstract
The MmpL family of proteins translocates complex (glyco)lipids and siderophores across the cell envelope of mycobacteria and closely related Corynebacteriaceae and plays important roles in the biogenesis of the outer membrane of these organisms. Despite their significance in the physiology and virulence of Mycobacterium tuberculosis, and from the perspective of developing novel antituberculosis agents, little is known about their structure and mechanism of translocation. In this study, the essential mycobacterial mycolic acid transporter, MmpL3, and its orthologue in Corynebacterium glutamicum, CmpL1, were investigated as prototypical MmpL proteins to gain insight into the transmembrane topo..
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Awarded by National Institute of Allergy and Infectious Diseases
Funding Acknowledgements
This work was supported by a grant from the Potts Memorial Foundation (to M.J.), by National Institutes of Health/National Institute of Allergy and Infectious Diseases Grants AI116525 (to M.J. and H.I.Z.) and AI092486 (to H.I.Z), and by GEPROM-FRSQ Intramural funding (to J.S., I.R., A.Y., and L.F.). The content is solely the responsibility of the authors and does not necessarily represent the official views of the NIH. We thank Dr. Michael Bott (Institut fur Bio- and Geowissenschaften, Germany) for the pAN6 expression plasmid. The Facility for Electron Microscopy Research at McGill University (FEMR) provided access to electron microscopes. Proteomics analyses were performed by the Center for Advanced Proteomics Analyses at the Universite de Montreal, a Node of the Canadian Genomic Innovation Network that is supported by the Canadian government through Genome Canada.