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Structures of the mycobacterial membrane protein MmpL3 reveal its mechanism of lipid transport
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Structures of the mycobacterial membrane protein MmpL3 reveal its mechanism of lipid transport
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Journal Article
Structures of the mycobacterial membrane protein MmpL3 reveal its mechanism of lipid transport
2021
Overview
The mycobacterial membrane protein large 3 (MmpL3) transporter is essential and required for shuttling the lipid trehalose monomycolate (TMM), a precursor of mycolic acid (MA)-containing trehalose dimycolate (TDM) and mycolyl arabinogalactan peptidoglycan (mAGP), in Mycobacterium species, including Mycobacterium tuberculosis and Mycobacterium smegmatis . However, the mechanism that MmpL3 uses to facilitate the transport of fatty acids and lipidic elements to the mycobacterial cell wall remains elusive. Here, we report 7 structures of the M . smegmatis MmpL3 transporter in its unbound state and in complex with trehalose 6-decanoate (T6D) or TMM using single-particle cryo-electron microscopy (cryo-EM) and X-ray crystallography. Combined with calculated results from molecular dynamics (MD) and target MD simulations, we reveal a lipid transport mechanism that involves a coupled movement of the periplasmic domain and transmembrane helices of the MmpL3 transporter that facilitates the shuttling of lipids to the mycobacterial cell wall.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
/ Bacterial Proteins - metabolism
/ Bacterial Proteins - ultrastructure
/ Helices
/ Lipids
/ Membrane Transport Proteins - metabolism
/ Membrane Transport Proteins - ultrastructure
/ Molecular Dynamics Simulation
/ Mycobacterium smegmatis - metabolism
/ Mycobacterium smegmatis - ultrastructure
/ Proteins
