3VMX

Crystal Structure of a parallel coiled-coil dimerization domain from the voltage-gated proton channel

3VMX の概要

• エントリーDOI: 10.2210/pdb3vmx/pdb
• 関連するPDBエントリー: 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, ion channel, ion transport, 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: 4
• 化学式量合計: 22394.00

構造登録者

Fujiwara, Y.,Takeshita, K.,Kobayashi, M.,Okamura, Y.,Nakagawa, A. (登録日: 2011-12-19, 公開日: 2012-05-30, 最終更新日: 2024-03-20)

主引用文献

Fujiwara, Y.,Kurokawa, T.,Takeshita, K.,Kobayashi, M.,Okochi, Y.,Nakagawa, A.,Okamura, Y.
The cytoplasmic coiled-coil mediates cooperative gating temperature sensitivity in the voltage-gated H(+) channel Hv1
Nat Commun, 3:816-816, 2012

PubMed Abstract: Hv1/VSOP is a dimeric voltage-gated H(+) channel in which the gating of one subunit is reportedly coupled to that of the other subunit within the dimer. The molecular basis for dimer formation and intersubunit coupling, however, remains unknown. Here we show that the carboxy terminus ends downstream of the S4 voltage-sensor helix twist in a dimer coiled-coil architecture, which mediates cooperative gating. We also show that the temperature-dependent activation of H(+) current through Hv1/VSOP is regulated by thermostability of the coiled-coil domain, and that this regulation is altered by mutation of the linker between S4 and the coiled-coil. Cooperative gating within the dimer is also dependent on the linker structure, which circular dichroism spectrum analysis suggests is α-helical. Our results indicate that the cytoplasmic coiled-coil strands form continuous α-helices with S4 and mediate cooperative gating to adjust the range of temperatures over which Hv1/VSOP operates.

PubMed: 22569364
DOI: 10.1038/ncomms1823

実験手法

X-RAY DIFFRACTION (1.45 Å)