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==Cryo-EM structure of VCCN1 in lipid nanodisc== | ==Cryo-EM structure of VCCN1 in lipid nanodisc== | ||
<StructureSection load='7ek2' size='340' side='right'caption='[[7ek2]]' scene=''> | <StructureSection load='7ek2' size='340' side='right'caption='[[7ek2]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EK2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ek2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EK2 FirstGlance]. <br> | ||
</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=7ek2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ek2 OCA], [https://pdbe.org/7ek2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ek2 RCSB], [https://www.ebi.ac.uk/pdbsum/7ek2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ek2 ProSAT]</span></td></tr> | </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=7ek2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ek2 OCA], [https://pdbe.org/7ek2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ek2 RCSB], [https://www.ebi.ac.uk/pdbsum/7ek2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ek2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In the light reaction of plant photosynthesis, modulation of electron transport chain reactions is important to maintain the efficiency of photosynthesis under a broad range of light intensities. VCCN1 was recently identified as a voltage-gated chloride channel residing in the thylakoid membrane, where it plays a key role in photoreaction tuning to avoid the generation of reactive oxygen species (ROS). Here, we present the cryo-EM structures of Malus domestica VCCN1 (MdVCCN1) in nanodiscs and detergent at 2.7 A and 3.0 A resolutions, respectively, and the structure-based electrophysiological analyses. VCCN1 structurally resembles its animal homolog, bestrophin, a Ca(2+)-gated anion channel. However, unlike bestrophin channels, VCCN1 lacks the Ca(2+)-binding motif but instead contains an N-terminal charged helix that is anchored to the lipid membrane through an additional amphipathic helix. Electrophysiological experiments demonstrate that these structural elements are essential for the channel activity, thus revealing the distinct activation mechanism of VCCN1. | |||
Cryo-EM structures of thylakoid-located voltage-dependent chloride channel VCCN1.,Hagino T, Kato T, Kasuya G, Kobayashi K, Kusakizako T, Hamamoto S, Sobajima T, Fujiwara Y, Yamashita K, Kawasaki H, Maturana AD, Nishizawa T, Nureki O Nat Commun. 2022 May 6;13(1):2505. doi: 10.1038/s41467-022-30292-w. PMID:35523970<ref>PMID:35523970</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7ek2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hagino T]] | [[Category: Hagino, T]] | ||
[[Category: Kasuya G]] | [[Category: Kasuya, G]] | ||
[[Category: Kato T]] | [[Category: Kato, T]] | ||
[[Category: Kobayashi K]] | [[Category: Kobayashi, K]] | ||
[[Category: Kusakizako T]] | [[Category: Kusakizako, T]] | ||
[[Category: Nishizawa T]] | [[Category: Nishizawa, T]] | ||
[[Category: Nureki O]] | [[Category: Nureki, O]] | ||
[[Category: Yamashita K]] | [[Category: Yamashita, K]] | ||
[[Category: Bestrophin family]] | |||
[[Category: Ion channel]] | |||
[[Category: Membrane protein]] | |||
[[Category: Photosynthesis]] | |||
[[Category: Thylakoid]] | |||
Revision as of 13:21, 18 May 2022
Cryo-EM structure of VCCN1 in lipid nanodiscCryo-EM structure of VCCN1 in lipid nanodisc
Structural highlights
Publication Abstract from PubMedIn the light reaction of plant photosynthesis, modulation of electron transport chain reactions is important to maintain the efficiency of photosynthesis under a broad range of light intensities. VCCN1 was recently identified as a voltage-gated chloride channel residing in the thylakoid membrane, where it plays a key role in photoreaction tuning to avoid the generation of reactive oxygen species (ROS). Here, we present the cryo-EM structures of Malus domestica VCCN1 (MdVCCN1) in nanodiscs and detergent at 2.7 A and 3.0 A resolutions, respectively, and the structure-based electrophysiological analyses. VCCN1 structurally resembles its animal homolog, bestrophin, a Ca(2+)-gated anion channel. However, unlike bestrophin channels, VCCN1 lacks the Ca(2+)-binding motif but instead contains an N-terminal charged helix that is anchored to the lipid membrane through an additional amphipathic helix. Electrophysiological experiments demonstrate that these structural elements are essential for the channel activity, thus revealing the distinct activation mechanism of VCCN1. Cryo-EM structures of thylakoid-located voltage-dependent chloride channel VCCN1.,Hagino T, Kato T, Kasuya G, Kobayashi K, Kusakizako T, Hamamoto S, Sobajima T, Fujiwara Y, Yamashita K, Kawasaki H, Maturana AD, Nishizawa T, Nureki O Nat Commun. 2022 May 6;13(1):2505. doi: 10.1038/s41467-022-30292-w. PMID:35523970[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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