8PNL

Outward-open conformation of a Major Facilitator Superfamily (MFS) transporter MHAS2168, a homologue of Rv1410 from M. tuberculosis, in complex with an alpaca nanobody

8PNL の概要

• エントリーDOI: 10.2210/pdb8pnl/pdb
• 分子名称: Putative triacylglyceride transporter, Nb_H2 (2 entities in total)
• 機能のキーワード: major facilitator superfamily transporter, nanobody, outward-open conformation, triacylglyceride extraction, transport protein
• 由来する生物種: Mycolicibacterium hassiacum DSM 44199; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 140233.03

構造登録者

Remm, S.,Schoeppe, J.,Hutter, C.A.J.,Gonda, I.,Seeger, M.A. (登録日: 2023-06-30, 公開日: 2023-10-18, 最終更新日: 2024-11-20)

主引用文献

Remm, S.,De Vecchis, D.,Schoppe, J.,Hutter, C.A.J.,Gonda, I.,Hohl, M.,Newstead, S.,Schafer, L.V.,Seeger, M.A.
Structural basis for triacylglyceride extraction from mycobacterial inner membrane by MFS transporter Rv1410.
Nat Commun, 14:6449-6449, 2023

PubMed Abstract: Mycobacterium tuberculosis is protected from antibiotic therapy by a multi-layered hydrophobic cell envelope. Major facilitator superfamily (MFS) transporter Rv1410 and the periplasmic lipoprotein LprG are involved in transport of triacylglycerides (TAGs) that seal the mycomembrane. Here, we report a 2.7 Å structure of a mycobacterial Rv1410 homologue, which adopts an outward-facing conformation and exhibits unusual transmembrane helix 11 and 12 extensions that protrude ~20 Å into the periplasm. A small, very hydrophobic cavity suitable for lipid transport is constricted by a functionally important ion-lock likely involved in proton coupling. Combining mutational analyses and MD simulations, we propose that TAGs are extracted from the core of the inner membrane into the central cavity via lateral clefts present in the inward-facing conformation. The functional role of the periplasmic helix extensions is to channel the extracted TAG into the lipid binding pocket of LprG.

PubMed: 37833269
DOI: 10.1038/s41467-023-42073-0

実験手法

X-RAY DIFFRACTION (2.7 Å)