3MKT

Structure of a Cation-bound Multidrug and Toxin Compound Extrusion (MATE) transporter

3MKT の概要

• エントリーDOI: 10.2210/pdb3mkt/pdb
• 関連するPDBエントリー: 3MKU
• 分子名称: Multi antimicrobial extrusion protein (Na(+)/drug antiporter) MATE-like MDR efflux pump (1 entity in total)
• 機能のキーワード: mate, multidrug transporter, cation-bound, transport protein
• 由来する生物種: Vibrio cholerae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 99522.27

構造登録者

He, X.,Szewczyk, P.,Karyakin, A.,Evin, M.,Hong, W.-X.,Zhang, Q.,Chang, G. (登録日: 2010-04-15, 公開日: 2010-09-29, 最終更新日: 2024-02-21)

主引用文献

He, X.,Szewczyk, P.,Karyakin, A.,Evin, M.,Hong, W.X.,Zhang, Q.,Chang, G.
Structure of a cation-bound multidrug and toxic compound extrusion transporter.
Nature, 467:991-994, 2010

PubMed Abstract: Transporter proteins from the MATE (multidrug and toxic compound extrusion) family are vital in metabolite transport in plants, directly affecting crop yields worldwide. MATE transporters also mediate multiple-drug resistance (MDR) in bacteria and mammals, modulating the efficacy of many pharmaceutical drugs used in the treatment of a variety of diseases. MATE transporters couple substrate transport to electrochemical gradients and are the only remaining class of MDR transporters whose structure has not been determined. Here we report the X-ray structure of the MATE transporter NorM from Vibrio cholerae determined to 3.65 Å, revealing an outward-facing conformation with two portals open to the outer leaflet of the membrane and a unique topology of the predicted 12 transmembrane helices distinct from any other known MDR transporter. We also report a cation-binding site in close proximity to residues previously deemed critical for transport. This conformation probably represents a stage of the transport cycle with high affinity for monovalent cations and low affinity for substrates.

PubMed: 20861838
DOI: 10.1038/nature09408

実験手法

X-RAY DIFFRACTION (3.65 Å)