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3vyi

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Current revision (08:43, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3vyi' size='340' side='right'caption='[[3vyi]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
<StructureSection load='3vyi' size='340' side='right'caption='[[3vyi]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vyi]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VYI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vyi]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VYI FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vmz|3vmz]], [[3vmy|3vmy]], [[3vmx|3vmx]], [[3vn0|3vn0]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.305&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hvcn1, Bts, Vsop ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vyi OCA], [https://pdbe.org/3vyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vyi RCSB], [https://www.ebi.ac.uk/pdbsum/3vyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vyi ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vyi OCA], [https://pdbe.org/3vyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vyi RCSB], [https://www.ebi.ac.uk/pdbsum/3vyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vyi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/HVCN1_MOUSE HVCN1_MOUSE]] Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagocytosis (By similarity).
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[https://www.uniprot.org/uniprot/HVCN1_MOUSE HVCN1_MOUSE] Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagocytosis (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Gating of the designed trimeric/tetrameric voltage-gated H+ channel.,Fujiwara Y, Kurokawa T, Takeshita K, Nakagawa A, Larsson HP, Okamura Y J Physiol. 2013 Feb 1;591(Pt 3):627-40. doi: 10.1113/jphysiol.2012.243006. Epub, 2012 Nov 19. PMID:23165764<ref>PMID:23165764</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3vyi" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Ion channels 3D structures|Ion channels 3D structures]]
*[[Ion channels 3D structures|Ion channels 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Fujiwara, Y]]
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[[Category: Fujiwara Y]]
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[[Category: Nakagawa, A]]
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[[Category: Nakagawa A]]
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[[Category: Takeshita, K]]
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[[Category: Takeshita K]]
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[[Category: Assembly]]
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[[Category: Coiled-coil]]
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[[Category: Cytoplasmic]]
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[[Category: Membrane protein]]
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Current revision

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

PDB ID 3vyi

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