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TitleStructural basis for ion selectivity in potassium-selective channelrhodopsins.
Journal, issue, pagesCell, Vol. 186, Issue 20, Page 4325-4344.e26, Year 2023
Publish dateSep 28, 2023
AuthorsSeiya Tajima / Yoon Seok Kim / Masahiro Fukuda / YoungJu Jo / Peter Y Wang / Joseph M Paggi / Masatoshi Inoue / Eamon F X Byrne / Koichiro E Kishi / Seiwa Nakamura / Charu Ramakrishnan / Shunki Takaramoto / Takashi Nagata / Masae Konno / Masahiro Sugiura / Kota Katayama / Toshiki E Matsui / Keitaro Yamashita / Suhyang Kim / Hisako Ikeda / Jaeah Kim / Hideki Kandori / Ron O Dror / Keiichi Inoue / Karl Deisseroth / Hideaki E Kato /
PubMed AbstractKCR channelrhodopsins (K-selective light-gated ion channels) have received attention as potential inhibitory optogenetic tools but more broadly pose a fundamental mystery regarding how their K ...KCR channelrhodopsins (K-selective light-gated ion channels) have received attention as potential inhibitory optogenetic tools but more broadly pose a fundamental mystery regarding how their K selectivity is achieved. Here, we present 2.5-2.7 Å cryo-electron microscopy structures of HcKCR1 and HcKCR2 and of a structure-guided mutant with enhanced K selectivity. Structural, electrophysiological, computational, spectroscopic, and biochemical analyses reveal a distinctive mechanism for K selectivity; rather than forming the symmetrical filter of canonical K channels achieving both selectivity and dehydration, instead, three extracellular-vestibule residues within each monomer form a flexible asymmetric selectivity gate, while a distinct dehydration pathway extends intracellularly. Structural comparisons reveal a retinal-binding pocket that induces retinal rotation (accounting for HcKCR1/HcKCR2 spectral differences), and design of corresponding KCR variants with increased K selectivity (KALI-1/KALI-2) provides key advantages for optogenetic inhibition in vitro and in vivo. Thus, discovery of a mechanism for ion-channel K selectivity also provides a framework for next-generation optogenetics.
External linksCell / PubMed:37652010 / PubMed Central
MethodsEM (single particle)
Resolution2.53 - 2.66 Å
Structure data

34530

8h86

EMDB-34530: Membrane protein A
PDB-8h86: Cryo-EM structure of the potassium-selective channelrhodopsin HcKCR1 in lipid nanodisc
Method: EM (single particle) / Resolution: 2.56 Å

34531

8h87

EMDB-34531: Membrane protein B
PDB-8h87: Cryo-EM structure of the potassium-selective channelrhodopsin HcKCR2 in lipid nanodisc
Method: EM (single particle) / Resolution: 2.53 Å

35713

8iu0

EMDB-35713, PDB-8iu0:
Cryo-EM structure of the potassium-selective channelrhodopsin HcKCR1 H225F mutant in lipid nanodisc
Method: EM (single particle) / Resolution: 2.66 Å

Chemicals

ChemComp-RET:
RETINAL / Retinal

ChemComp-PSC:
(7R,17E,20E)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSA-17,20-DIEN-1-AMINIUM 4-OXIDE / phospholipid*YM / Phosphatidylcholine

ChemComp-PLM:
PALMITIC ACID / Palmitic acid

ChemComp-HOH:
WATER / Water

Source
  • hyphochytrium catenoides (eukaryote)
KeywordsMEMBRANE PROTEIN / Cryo-EM

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