7K8C

CryoEM structure of a trehalose monomycolate transporter in lipid nanodiscs

7K8C の概要

• エントリーDOI: 10.2210/pdb7k8c/pdb
• EMDBエントリー: 22724 22726
• 分子名称: Trehalose monomycolate exporter MmpL3 (1 entity in total)
• 機能のキーワード: trehalose monomycolate transporter, translocase
• 由来する生物種: Mycolicibacterium smegmatis (Mycobacterium smegmatis)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 109509.22

構造登録者

Su, C.-C. (登録日: 2020-09-26, 公開日: 2021-09-22, 最終更新日: 2025-05-28)

主引用文献

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

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

実験手法

ELECTRON MICROSCOPY (4.27 Å)