7N6B
Structure of MmpL3 reconstituted into lipid nanodisc in the TMM bound state
Summary for 7N6B
| Entry DOI | 10.2210/pdb7n6b/pdb |
| EMDB information | 24206 |
| Descriptor | MmpL3 transporter, 6-O-[(2S)-2-{(1S)-18-[(1R,2R)-2-hexylcyclopropyl]-1-hydroxyoctadecyl}tricosanoyl]-alpha-D-glucopyranosyl alpha-D-glucopyranoside (2 entities in total) |
| Functional Keywords | transporter, translocase |
| Biological source | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
| Total number of polymer chains | 1 |
| Total formula weight | 111652.40 |
| Authors | |
| Primary citation | Su, C.C.,Klenotic, P.A.,Cui, M.,Lyu, M.,Morgan, C.E.,Yu, E.W. Structures of the mycobacterial membrane protein MmpL3 reveal its mechanism of lipid transport. Plos Biol., 19:e3001370-e3001370, 2021 Cited by PubMed Abstract: 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. PubMed: 34383749DOI: 10.1371/journal.pbio.3001370 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.66 Å) |
Structure validation
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