6A6M

Crystal structure of an outward-open nucleotide-bound state of the eukaryotic ABC multidrug transporter CmABCB1

6A6M の概要

• エントリーDOI: 10.2210/pdb6a6m/pdb
• 分子名称: ATP-binding cassette, sub-family B, member 1, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: transport protein alpha-helical, transport protein
• 由来する生物種: Cyanidioschyzon merolae strain 10D (Red alga)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 68086.80

構造登録者

Kato, H.,Nakatsu, T.,Kodan, A. (登録日: 2018-06-28, 公開日: 2019-02-20, 最終更新日: 2024-03-27)

主引用文献

Kodan, A.,Yamaguchi, T.,Nakatsu, T.,Matsuoka, K.,Kimura, Y.,Ueda, K.,Kato, H.
Inward- and outward-facing X-ray crystal structures of homodimeric P-glycoprotein CmABCB1.
Nat Commun, 10:88-88, 2019

PubMed Abstract: P-glycoprotein extrudes a large variety of xenobiotics from the cell, thereby protecting tissues from their toxic effects. The machinery underlying unidirectional multidrug pumping remains unknown, largely due to the lack of high-resolution structural information regarding the alternate conformational states of the molecule. Here we report a pair of structures of homodimeric P-glycoprotein: an outward-facing conformational state with bound nucleotide and an inward-facing apo state, at resolutions of 1.9 Å and 3.0 Å, respectively. Features that can be clearly visualized at this high resolution include ATP binding with octahedral coordination of Mg; an inner chamber that significantly changes in volume with the aid of tight connections among transmembrane helices (TM) 1, 3, and 6; a glutamate-arginine interaction that stabilizes the outward-facing conformation; and extensive interactions between TM1 and TM3, a property that distinguishes multidrug transporters from floppases. These structural elements are proposed to participate in the mechanism of the transporter.

PubMed: 30622258
DOI: 10.1038/s41467-018-08007-x

実験手法

X-RAY DIFFRACTION (1.9 Å)