5EBM

KcsA T75G mutant in the nonconductive state

5EBM の概要

• エントリーDOI: 10.2210/pdb5ebm/pdb
• 関連するPDBエントリー: 5EBL 5EBW 5EC1 5EC2
• 分子名称: Antibody Fab Fragment Light Chain, pH-gated potassium channel KcsA, DIACYL GLYCEROL, ... (7 entities in total)
• 機能のキーワード: alpha-helical, membrane protein, fab, channel
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 60943.18

構造登録者

Matulef, K.,Valiyaveetil, F.I. (登録日: 2015-10-19, 公開日: 2016-04-20, 最終更新日: 2023-09-27)

主引用文献

Matulef, K.,Annen, A.W.,Nix, J.C.,Valiyaveetil, F.I.
Individual Ion Binding Sites in the K(+) Channel Play Distinct Roles in C-type Inactivation and in Recovery from Inactivation.
Structure, 24:750-761, 2016

PubMed Abstract: The selectivity filter of K(+) channels contains four ion binding sites (S1-S4) and serves dual functions of discriminating K(+) from Na(+) and acting as a gate during C-type inactivation. C-type inactivation is modulated by ion binding to the selectivity filter sites, but the underlying mechanism is not known. Here we evaluate how the ion binding sites in the selectivity filter of the KcsA channel participate in C-type inactivation and in recovery from inactivation. We use unnatural amide-to-ester substitutions in the protein backbone to manipulate the S1-S3 sites and a side-chain substitution to perturb the S4 site. We develop an improved semisynthetic approach for generating these amide-to-ester substitutions in the selectivity filter. Our combined electrophysiological and X-ray crystallographic analysis of the selectivity filter mutants show that the ion binding sites play specific roles during inactivation and provide insights into the structural changes at the selectivity filter during C-type inactivation.

PubMed: 27150040
DOI: 10.1016/j.str.2016.02.021

実験手法

X-RAY DIFFRACTION (2.5 Å)