4LZ6

Structure of MATE multidrug transporter DinF-BH

4LZ6 の概要

• エントリーDOI: 10.2210/pdb4lz6/pdb
• 関連するPDBエントリー: 4LZ9
• 分子名称: BH2163 protein (1 entity in total)
• 機能のキーワード: multidrug transporter, transport protein
• 由来する生物種: Bacillus halodurans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48615.17

構造登録者

Lu, M.,Radchenko, M.,Symersky, J.,Nie, R.,Guo, Y. (登録日: 2013-07-31, 公開日: 2013-10-23, 最終更新日: 2024-03-20)

主引用文献

Lu, M.,Radchenko, M.,Symersky, J.,Nie, R.,Guo, Y.
Structural insights into H(+)-coupled multidrug extrusion by a MATE transporter
Nat.Struct.Mol.Biol., 20:1310-1317, 2013

PubMed Abstract: Multidrug and toxic compound extrusion (MATE) transporters contribute to multidrug resistance by coupling the efflux of drugs to the influx of Na(+) or H(+). Known structures of Na(+)-coupled, extracellular-facing MATE transporters from the NorM subfamily revealed 12 membrane-spanning segments related by a quasi-two-fold rotational symmetry and a multidrug-binding cavity situated near the membrane surface. Here we report the crystal structure of an H(+)-coupled MATE transporter from Bacillus halodurans and the DinF subfamily at 3.2-Å resolution, unveiling a surprisingly asymmetric arrangement of 12 transmembrane helices. We also identified a membrane-embedded substrate-binding chamber by combining crystallographic and biochemical analyses. Our studies further suggested a direct competition between H(+) and substrate during DinF-mediated transport and implied how a MATE transporter alternates between its extracellular- and intracellular-facing conformations to propel multidrug extrusion. Collectively, our results demonstrated heretofore-unrecognized mechanistic diversity among MATE transporters.

PubMed: 24141706
DOI: 10.1038/nsmb.2687

実験手法

X-RAY DIFFRACTION (3.2 Å)