4LP8

A Novel Open-State Crystal Structure of the Prokaryotic Inward Rectifier KirBac3.1

4LP8 の概要

• エントリーDOI: 10.2210/pdb4lp8/pdb
• 関連するPDBエントリー: 3ZRS
• 分子名称: Inward rectifier potassium channel Kirbac3.1, DI(HYDROXYETHYL)ETHER, POTASSIUM ION, ... (5 entities in total)
• 機能のキーワード: metal transport, potassium channel, membrane
• 由来する生物種: Magnetospirillum magnetotacticum
• 細胞内の位置: Membrane; Multi-pass membrane protein: D9N164
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34404.22

構造登録者

Zubcevic, L.,Bavro, V.N.,Muniz, J.R.C.,Schmidt, M.R.,Wang, S.,De Zorzi, R.,Venien-Bryan, C.,Sansom, M.S.P.,Nichols, C.G.,Tucker, S.J. (登録日: 2013-07-15, 公開日: 2013-11-20, 最終更新日: 2023-09-20)

主引用文献

Zubcevic, L.,Bavro, V.N.,Muniz, J.R.,Schmidt, M.R.,Wang, S.,De Zorzi, R.,Venien-Bryan, C.,Sansom, M.S.,Nichols, C.G.,Tucker, S.J.
Control of KirBac3.1 Potassium Channel Gating at the Interface between Cytoplasmic Domains.
J.Biol.Chem., 289:143-151, 2014

PubMed Abstract: KirBac channels are prokaryotic homologs of mammalian inwardly rectifying potassium (Kir) channels, and recent structures of KirBac3.1 have provided important insights into the structural basis of gating in Kir channels. In this study, we demonstrate that KirBac3.1 channel activity is strongly pH-dependent, and we used x-ray crystallography to determine the structural changes that arise from an activatory mutation (S205L) located in the cytoplasmic domain (CTD). This mutation stabilizes a novel energetically favorable open conformation in which changes at the intersubunit interface in the CTD also alter the electrostatic potential of the inner cytoplasmic cavity. These results provide a structural explanation for the activatory effect of this mutation and provide a greater insight into the role of the CTD in Kir channel gating.

PubMed: 24257749
DOI: 10.1074/jbc.M113.501833

実験手法

X-RAY DIFFRACTION (2.46 Å)