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3VYI

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

Summary for 3VYI
Entry DOI10.2210/pdb3vyi/pdb
Related3VMX 3VMY 3VMZ 3VN0
DescriptorVoltage-gated hydrogen channel 1 (2 entities in total)
Functional Keywordscoiled-coil, assembly, cytoplasmic, membrane protein
Biological sourceMus musculus (mouse)
Cellular locationMembrane; Multi-pass membrane protein: Q3U2S8
Total number of polymer chains12
Total formula weight71061.14
Authors
Fujiwara, Y.,Takeshita, K.,Nakagawa, A. (deposition date: 2012-09-25, release date: 2013-02-27, Last modification date: 2024-03-20)
Primary citationFujiwara, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.305 Å)
Structure validation

246031

数据于2025-12-10公开中

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