3VMX

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

Summary for 3VMX

• Entry DOI: 10.2210/pdb3vmx/pdb
• Related: 3VMY 3VMZ 3VN0
• Descriptor: Voltage-gated hydrogen channel 1 (2 entities in total)
• Functional Keywords: coiled-coil, ion channel, ion transport, membrane protein
• Biological source: Mus musculus (mouse)
• Cellular location: Membrane; Multi-pass membrane protein: Q3U2S8
• Total number of polymer chains: 4
• Total formula weight: 22394.00

Authors

Fujiwara, Y.,Takeshita, K.,Kobayashi, M.,Okamura, Y.,Nakagawa, A. (deposition date: 2011-12-19, release date: 2012-05-30, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.45 Å)