6GWH

Outward-facing conformation of a multidrug resistance MATE family transporter of the MOP superfamily.

6GWH の概要

• エントリーDOI: 10.2210/pdb6gwh/pdb
• 分子名称: MOP transporter (1 entity in total)
• 機能のキーワード: mop flippase, membrane protein
• 由来する生物種: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49276.26

構造登録者

Zakrzewska, S.,Safarian, S.,Michel, H. (登録日: 2018-06-25, 公開日: 2019-06-05, 最終更新日: 2024-01-17)

主引用文献

Zakrzewska, S.,Mehdipour, A.R.,Malviya, V.N.,Nonaka, T.,Koepke, J.,Muenke, C.,Hausner, W.,Hummer, G.,Safarian, S.,Michel, H.
Inward-facing conformation of a multidrug resistance MATE family transporter.
Proc.Natl.Acad.Sci.USA, 116:12275-12284, 2019

PubMed Abstract: Multidrug and toxic compound extrusion (MATE) transporters mediate excretion of xenobiotics and toxic metabolites, thereby conferring multidrug resistance in bacterial pathogens and cancer cells. Structural information on the alternate conformational states and knowledge of the detailed mechanism of MATE transport are of great importance for drug development. However, the structures of MATE transporters are only known in V-shaped outward-facing conformations. Here, we present the crystal structure of a MATE transporter from (PfMATE) in the long-sought-after inward-facing state, which was obtained after crystallization in the presence of native lipids. Transition from the outward-facing state to the inward-facing state involves rigid body movements of transmembrane helices (TMs) 2-6 and 8-12 to form an inverted V, facilitated by a loose binding of TM1 and TM7 to their respective bundles and their conformational flexibility. The inward-facing structure of PfMATE in combination with the outward-facing one supports an alternating access mechanism for the MATE family transporters.

PubMed: 31160466
DOI: 10.1073/pnas.1904210116

実験手法

X-RAY DIFFRACTION (2.8 Å)