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Structure paper

TitleStructural insights into light-gating of potassium-selective channelrhodopsin.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 1283, Year 2025
Publish dateFeb 3, 2025
AuthorsTakefumi Morizumi / Kyumhyuk Kim / Hai Li / Probal Nag / Tal Dogon / Oleg A Sineshchekov / Yumei Wang / Leonid S Brown / Songhwan Hwang / Han Sun / Ana-Nicoleta Bondar / Igor Schapiro / Elena G Govorunova / John L Spudich / Oliver P Ernst /
PubMed AbstractStructural information on channelrhodopsins' mechanism of light-gated ion conductance is scarce, limiting its engineering as optogenetic tools. Here, we use single-particle cryo-electron microscopy ...Structural information on channelrhodopsins' mechanism of light-gated ion conductance is scarce, limiting its engineering as optogenetic tools. Here, we use single-particle cryo-electron microscopy of peptidisc-incorporated protein samples to determine the structures of the slow-cycling mutant C110A of kalium channelrhodopsin 1 from Hyphochytrium catenoides (HcKCR1) in the dark and upon laser flash excitation. Upon photoisomerization of the retinal chromophore, the retinylidene Schiff base NH-bond reorients from the extracellular to the cytoplasmic side. This switch triggers a series of side chain reorientations and merges intramolecular cavities into a transmembrane K conduction pathway. Molecular dynamics simulations confirm K flux through the illuminated state but not through the resting state. The overall displacement between the closed and the open structure is small, involving mainly side chain rearrangements. Asp105 and Asp116 play a key role in K conductance. Structure-guided mutagenesis and patch-clamp analysis reveal the roles of the pathway-forming residues in channel gating and selectivity.
External linksNat Commun / PubMed:39900567 / PubMed Central
MethodsEM (single particle)
Resolution3.05 - 3.44 Å
Structure data

45467

9cdc

EMDB-45467, PDB-9cdc:
Kalium channelrhodopsin 1 C110A mutant from Hyphochytrium catenoides, Dark State
Method: EM (single particle) / Resolution: 3.08 Å

45468

9cdd

EMDB-45468, PDB-9cdd:
Kalium channelrhodopsin 1 C110A mutant from Hyphochytrium catenoides, Laser-Flash-Illuminated
Method: EM (single particle) / Resolution: 3.05 Å

45469

9cde

EMDB-45469, PDB-9cde:
Kalium channelrhodopsin 1 C110A mutant from Hyphochytrium catenoides, Continuous Illumination State
Method: EM (single particle) / Resolution: 3.44 Å

Chemicals

ChemComp-RET:
RETINAL

ChemComp-CLR:
CHOLESTEROL

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM

ChemComp-HOH:
WATER

Source
  • hyphochytrium catenoides (eukaryote)
KeywordsMEMBRANE PROTEIN / Retinal Protein / Channelrhodopsin / Cation Channel / Peptidisc / Optogenetics / Transport Protein

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