5BUT

Crystal structure of inactive conformation of KtrAB K+ transporter

5BUT の概要

• エントリーDOI: 10.2210/pdb5but/pdb
• 分子名称: Ktr system potassium uptake protein A,Ktr system potassium uptake protein A, Ktr system potassium uptake protein B, POTASSIUM ION (3 entities in total)
• 機能のキーワード: membrane protein complex, membrane protein
• 由来する生物種: Bacillus subtilis; 詳細
• 細胞内の位置: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : O32080; Cell membrane ; Multi-pass membrane protein : O32081
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 320943.42

構造登録者

Vieira-Pires, R.S.,Morais-Cabral, J.H. (登録日: 2015-06-04, 公開日: 2016-01-27, 最終更新日: 2024-01-10)

主引用文献

Szollosi, A.,Vieira-Pires, R.S.,Teixeira-Duarte, C.M.,Rocha, R.,Morais-Cabral, J.H.
Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter.
Plos Biol., 14:e1002356-e1002356, 2016

PubMed Abstract: KtrAB belongs to the Trk/Ktr/HKT superfamily of monovalent cation (K+ and Na+) transport proteins that closely resemble K+ channels. These proteins underlie a plethora of cellular functions that are crucial for environmental adaptation in plants, fungi, archaea, and bacteria. The activation mechanism of the Trk/Ktr/HKT proteins remains unknown. It has been shown that ATP stimulates the activity of KtrAB while ADP does not. Here, we present X-ray structural information on the KtrAB complex with bound ADP. A comparison with the KtrAB-ATP structure reveals conformational changes in the ring and in the membrane protein. In combination with a biochemical and functional analysis, we uncover how ligand-dependent changes in the KtrA ring are propagated to the KtrB membrane protein and conclude that, despite their structural similarity, the activation mechanism of KtrAB is markedly different from the activation mechanism of K+ channels.

PubMed: 26771197
DOI: 10.1371/journal.pbio.1002356

実験手法

X-RAY DIFFRACTION (5.97 Å)