6GV1

Crystal structure of E.coli Multidrug/H+ antiporter MdfA in outward open conformation with bound Fab fragment

6GV1 の概要

• エントリーDOI: 10.2210/pdb6gv1/pdb
• 分子名称: Major Facilitator Superfamily multidrug/H+ antiporter MdfA from E.coli, Fab fragment YN1074 heavy chain, Fab fragment YN1074 light chain, ... (4 entities in total)
• 機能のキーワード: major facilitator superfamily, multidrug resistance, proton transport, mfs transporter, drug proton antiporter, transport protein
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 93062.93

構造登録者

Nagarathinam, K.,Parthier, C.,Stubbs, M.T.,Tanabe, M. (登録日: 2018-06-20, 公開日: 2018-10-03, 最終更新日: 2024-10-09)

主引用文献

Nagarathinam, K.,Nakada-Nakura, Y.,Parthier, C.,Terada, T.,Juge, N.,Jaenecke, F.,Liu, K.,Hotta, Y.,Miyaji, T.,Omote, H.,Iwata, S.,Nomura, N.,Stubbs, M.T.,Tanabe, M.
Outward open conformation of a Major Facilitator Superfamily multidrug/H+antiporter provides insights into switching mechanism.
Nat Commun, 9:4005-4005, 2018

PubMed Abstract: Multidrug resistance (MDR) poses a major challenge to medicine. A principle cause of MDR is through active efflux by MDR transporters situated in the bacterial membrane. Here we present the crystal structure of the major facilitator superfamily (MFS) drug/H antiporter MdfA from Escherichia coli in an outward open conformation. Comparison with the inward facing (drug binding) state shows that, in addition to the expected change in relative orientations of the N- and C-terminal lobes of the antiporter, the conformation of TM5 is kinked and twisted. In vitro reconstitution experiments demonstrate the importance of selected residues for transport and molecular dynamics simulations are used to gain insights into antiporter switching. With the availability of structures of alternative conformational states, we anticipate that MdfA will serve as a model system for understanding drug efflux in MFS MDR antiporters.

PubMed: 30275448
DOI: 10.1038/s41467-018-06306-x

実験手法

X-RAY DIFFRACTION (3.4 Å)