3VYI

Crystal Structure of a trimeric coiled-coil (I/I-type) assembly domain from the voltage-gated proton channel mutant

3VYI の概要

• エントリーDOI: 10.2210/pdb3vyi/pdb
• 関連するPDBエントリー: 3VMX 3VMY 3VMZ 3VN0
• 分子名称: Voltage-gated hydrogen channel 1 (2 entities in total)
• 機能のキーワード: coiled-coil, assembly, cytoplasmic, membrane protein
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Membrane; Multi-pass membrane protein: Q3U2S8
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 71061.14

構造登録者

Fujiwara, Y.,Takeshita, K.,Nakagawa, A. (登録日: 2012-09-25, 公開日: 2013-02-27, 最終更新日: 2024-03-20)

主引用文献

Fujiwara, Y.,Kurokawa, T.,Takeshita, K.,Nakagawa, A.,Larsson, H.P.,Okamura, Y.
Gating of the designed trimeric/tetrameric voltage-gated H+ channel.
J.Physiol.(Paris), 591:627-640, 2013

PubMed Abstract: The voltage-gated H(+) channel functions as a dimer, a configuration that is different from standard tetrameric voltage-gated channels. Each channel protomer has its own permeation pathway. The C-terminal coiled-coil domain has been shown to be necessary for both dimerization and cooperative gating in the two channel protomers. Here we report the gating cooperativity in trimeric and tetrameric Hv channels engineered by altering the hydrophobic core sequence of the coiled-coil assembly domain. Trimeric and tetrameric channels exhibited more rapid and less sigmoidal kinetics of activation of H(+) permeation than dimeric channels, suggesting that some channel protomers in trimers and tetramers failed to produce gating cooperativity observed in wild-type dimers. Multimerization of trimer and tetramer channels were confirmed by the biochemical analysis of proteins, including crystallography. These findings indicate that the voltage-gated H(+) channel is optimally designed as a dimeric channel on a solid foundation of the sequence pattern of the coiled-coil core, with efficient cooperative gating that ensures sustained and steep voltage-dependent H(+) conductance in blood cells.

PubMed: 23165764
DOI: 10.1113/jphysiol.2012.243006

実験手法

X-RAY DIFFRACTION (2.305 Å)