9DP6

Mycolicibacterium smegmatis MmpL5-AcpM structure

9DP6 の概要

• エントリーDOI: 10.2210/pdb9dp6/pdb
• EMDBエントリー: 47097
• 分子名称: Meromycolate extension acyl carrier protein, MmpL5 protein, 4'-PHOSPHOPANTETHEINE (3 entities in total)
• 機能のキーワード: mycolicibacterium smegmatis, mmpl5, acpm, transport protein
• 由来する生物種: Mycolicibacterium smegmatis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 116700.44

構造登録者

Maharjan, R.,Klenotic, P.A.,Zhang, Z.,Yu, E.W. (登録日: 2024-09-20, 公開日: 2024-10-23, 最終更新日: 2025-05-28)

主引用文献

Maharjan, R.,Zhang, Z.,Klenotic, P.A.,Gregor, W.D.,Tringides, M.L.,Cui, M.,Purdy, G.E.,Yu, E.W.
Structures of the mycobacterial MmpL4 and MmpL5 transporters provide insights into their role in siderophore export and iron acquisition.
Plos Biol., 22:e3002874-e3002874, 2024

PubMed Abstract: The Mycobacterium tuberculosis (Mtb) pathogen, the causative agent of the airborne infection tuberculosis (TB), harbors a number of mycobacterial membrane protein large (MmpL) transporters. These membrane proteins can be separated into 2 distinct subclasses, where they perform important functional roles, and thus, are considered potential drug targets to combat TB. Previously, we reported both X-ray and cryo-EM structures of the MmpL3 transporter, providing high-resolution structural information for this subclass of the MmpL proteins. Currently, there is no structural information available for the subclass associated with MmpL4 and MmpL5, transporters that play a critical role in iron homeostasis of the bacterium. Here, we report cryo-EM structures of the M. smegmatis MmpL4 and MmpL5 transporters to resolutions of 2.95 Å and 3.00 Å, respectively. These structures allow us to propose a plausible pathway for siderophore translocation via these 2 transporters, an essential step for iron acquisition that enables the survival and replication of the mycobacterium.

PubMed: 39423221
DOI: 10.1371/journal.pbio.3002874

実験手法

ELECTRON MICROSCOPY (2.81 Å)