3EYW

Crystal structure of the C-terminal domain of E. coli KefC in complex with KefF

3EYW の概要

• エントリーDOI: 10.2210/pdb3eyw/pdb
• 分子名称: C-terminal domain of Glutathione-regulated potassium-efflux system protein kefC fused to full length Glutathione-regulated potassium-efflux system ancillary protein kefF, FLAVIN MONONUCLEOTIDE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (6 entities in total)
• 機能のキーワード: ktn, rck, k+ channel, k+ transport, kefc, k+ efflux, channel regulation, antiport, inner membrane, ion transport, membrane, potassium, potassium transport, transmembrane, transport protein
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cell inner membrane ; Peripheral membrane protein ; Cytoplasmic side : P0A754
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 95510.35

構造登録者

Roosild, T.P. (登録日: 2008-10-22, 公開日: 2009-06-30, 最終更新日: 2023-09-06)

主引用文献

Roosild, T.P.,Castronovo, S.,Miller, S.,Li, C.,Rasmussen, T.,Bartlett, W.,Gunasekera, B.,Choe, S.,Booth, I.R.
KTN (RCK) Domains Regulate K(+) Channels and Transporters by Controlling the Dimer-Hinge Conformation.
Structure, 17:893-903, 2009

PubMed Abstract: KTN (RCK) domains are nucleotide-binding folds that form the cytoplasmic regulatory complexes of various K+ channels and transporters. The mechanisms these proteins use to control their transmembrane pore-forming counterparts remains unclear despite numerous electrophysiological and structural studies. KTN (RCK) domains consistently crystallize as dimers within the asymmetric unit, forming a pronounced hinge between two Rossmann folds. We have previously proposed that modification of the hinge angle plays an important role in activating the associated membrane-integrated components of the channel or transporter. Here we report the structure of the C-terminal, KTN-bearing domain of the E. coli KefC K+ efflux system in association with the ancillary subunit, KefF, which is known to stabilize the conductive state. The structure of the complex and functional analysis of KefC variants reveal that control of the conformational flexibility inherent in the KTN dimer hinge is modulated by KefF and essential for regulation of KefC ion flux.

PubMed: 19523906
DOI: 10.1016/j.str.2009.03.018

実験手法

X-RAY DIFFRACTION (2.4 Å)