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Structure paper

TitleStructural basis for channel conduction in the pump-like channelrhodopsin ChRmine.
Journal, issue, pagesCell, Vol. 185, Issue 4, Page 672-689.e23, Year 2022
Publish dateFeb 17, 2022
AuthorsKoichiro E Kishi / Yoon Seok Kim / Masahiro Fukuda / Masatoshi Inoue / Tsukasa Kusakizako / Peter Y Wang / Charu Ramakrishnan / Eamon F X Byrne / Elina Thadhani / Joseph M Paggi / Toshiki E Matsui / Keitaro Yamashita / Takashi Nagata / Masae Konno / Sean Quirin / Maisie Lo / Tyler Benster / Tomoko Uemura / Kehong Liu / Mikihiro Shibata / Norimichi Nomura / So Iwata / Osamu Nureki / Ron O Dror / Keiichi Inoue / Karl Deisseroth / Hideaki E Kato /
PubMed AbstractChRmine, a recently discovered pump-like cation-conducting channelrhodopsin, exhibits puzzling properties (large photocurrents, red-shifted spectrum, and extreme light sensitivity) that have created ...ChRmine, a recently discovered pump-like cation-conducting channelrhodopsin, exhibits puzzling properties (large photocurrents, red-shifted spectrum, and extreme light sensitivity) that have created new opportunities in optogenetics. ChRmine and its homologs function as ion channels but, by primary sequence, more closely resemble ion pump rhodopsins; mechanisms for passive channel conduction in this family have remained mysterious. Here, we present the 2.0 Å resolution cryo-EM structure of ChRmine, revealing architectural features atypical for channelrhodopsins: trimeric assembly, a short transmembrane-helix 3, a twisting extracellular-loop 1, large vestibules within the monomer, and an opening at the trimer interface. We applied this structure to design three proteins (rsChRmine and hsChRmine, conferring further red-shifted and high-speed properties, respectively, and frChRmine, combining faster and more red-shifted performance) suitable for fundamental neuroscience opportunities. These results illuminate the conduction and gating of pump-like channelrhodopsins and point the way toward further structure-guided creation of channelrhodopsins for applications across biology.
External linksCell / PubMed:35114111 / PubMed Central
MethodsEM (single particle)
Resolution2.02 - 2.12 Å
Structure data

32377

7w9w

EMDB-32377, PDB-7w9w:
2.02 angstrom cryo-EM structure of the pump-like channelrhodopsin ChRmine
Method: EM (single particle) / Resolution: 2.02 Å

EMDB-32378:
2.12 angstrom cryo-EM map of the pump-like channelrhodopsin ChRmine with Fab antibody fragment
Method: EM (single particle) / Resolution: 2.12 Å

Chemicals

ChemComp-RET:
RETINAL / Retinal

ChemComp-CLR:
CHOLESTEROL / Cholesterol

ChemComp-PLM:
PALMITIC ACID / Palmitic acid

ChemComp-HOH:
WATER / Water

Source
  • rhodomonas lens (eukaryote)
KeywordsMEMBRANE PROTEIN / channelrhodopsin / ion channel / photoreceptor / cryo-EM

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