5YCK

Crystal structure of a MATE family protein derived from Camelina sativa at 2.3 angstrom

5YCK の概要

• エントリーDOI: 10.2210/pdb5yck/pdb
• 関連するPDBエントリー: 5XJJ
• 分子名称: multi drug efflux transporter, RUBIDIUM ION, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (4 entities in total)
• 機能のキーワード: membrane protein, multi drug resistance, transporter, transport protein
• 由来する生物種: Camelina sativa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52667.19

構造登録者

Tanaka, Y.,Tsukazaki, T.,Iwaki, S. (登録日: 2017-09-07, 公開日: 2017-09-27, 最終更新日: 2023-11-22)

主引用文献

Tanaka, Y.,Iwaki, S.,Tsukazaki, T.
Crystal Structure of a Plant Multidrug and Toxic Compound Extrusion Family Protein
Structure, 25:1455-1460.e2, 2017

PubMed Abstract: The multidrug and toxic compound extrusion (MATE) family of proteins consists of transporters responsible for multidrug resistance in prokaryotes. In plants, a number of MATE proteins were identified by recent genomic and functional studies, which imply that the proteins have substrate-specific transport functions instead of multidrug extrusion. The three-dimensional structure of eukaryotic MATE proteins, including those of plants, has not been reported, preventing a better understanding of the molecular mechanism of these proteins. Here, we describe the crystal structure of a MATE protein from the plant Camelina sativa at 2.9 Å resolution. Two sets of six transmembrane α helices, assembled pseudo-symmetrically, possess a negatively charged internal pocket with an outward-facing shape. The crystal structure provides insight into the diversity of plant MATE proteins and their substrate recognition and transport through the membrane.

PubMed: 28877507
DOI: 10.1016/j.str.2017.07.009

実験手法

X-RAY DIFFRACTION (2.3 Å)