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TitleStructures of the mycobacterial membrane protein MmpL3 reveal its mechanism of lipid transport.
Journal, issue, pagesPLoS Biol, Vol. 19, Issue 8, Page e3001370, Year 2021
Publish dateAug 12, 2021
AuthorsChih-Chia Su / Philip A Klenotic / Meng Cui / Meinan Lyu / Christopher E Morgan / Edward W Yu /
PubMed AbstractThe 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 ...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.
External linksPLoS Biol / PubMed:34383749 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.66 - 4.33 Å
Structure data

EMDB-22724, PDB-7k8a:
CryoEM structure of a trehalose monomycolate transporter in lipid nanodiscs
Method: EM (single particle) / Resolution: 3.65 Å

EMDB-22725, PDB-7k8b:
CryoEM structure of a trehalose monomycolate transporter in lipid nanodiscs
Method: EM (single particle) / Resolution: 2.94 Å

EMDB-22726, PDB-7k8c:
CryoEM structure of a trehalose monomycolate transporter in lipid nanodiscs
Method: EM (single particle) / Resolution: 4.27 Å

EMDB-22728, PDB-7k8d:
CryoEM structure of a trehalose monomycolate transporter in TMM lipid nanodiscs (form II)
Method: EM (single particle) / Resolution: 4.33 Å

EMDB-24206, PDB-7n6b:
Structure of MmpL3 reconstituted into lipid nanodisc in the TMM bound state
Method: EM (single particle) / Resolution: 2.66 Å

PDB-7k7m:
Crystal Structure of a membrane protein
Method: X-RAY DIFFRACTION / Resolution: 3.33 Å

Chemicals

ChemComp-0HJ:
6-O-[(2S)-2-{(1S)-18-[(1R,2R)-2-hexylcyclopropyl]-1-hydroxyoctadecyl}tricosanoyl]-alpha-D-glucopyranosyl alpha-D-glucopyranoside

Source
  • mycolicibacterium smegmatis (bacteria)
  • mycolicibacterium smegmatis (strain atcc 700084 / mc(2)155) (bacteria)
KeywordsMEMBRANE PROTEIN / transporter / TRANSLOCASE / trehalose monomycolate transporter

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