Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7N6B

Structure of MmpL3 reconstituted into lipid nanodisc in the TMM bound state

Summary for 7N6B
Entry DOI10.2210/pdb7n6b/pdb
EMDB information24206
DescriptorMmpL3 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 Keywordstransporter, translocase
Biological sourceMycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Total number of polymer chains1
Total formula weight111652.40
Authors
Su, C.C.,Yu, E. (deposition date: 2021-06-08, release date: 2021-09-01, Last modification date: 2024-05-29)
Primary citationSu, 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: 34383749
DOI: 10.1371/journal.pbio.3001370
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.66 Å)
Structure validation

226707

數據於2024-10-30公開中

PDB statisticsPDBj update infoContact PDBjnumon