3.E.1.7.11 ChRmine of 318 aas and 7 TMSs. It is a pump-like cation-conducting channelrhodopsin that 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; Kishi et al. 2022 presented 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. The authors 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 (Kishi et al. 2022).
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Accession Number: | 7SFJ-A |
Protein Name: | A Chain A, ChRmine |
Length: | 319 |
Molecular Weight: | |
Species: | Tiarina fusa [693140] |
Number of TMSs: | 7 |
Substrate |
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1: MXHAPGTDQM FYVGTMDGWY LDTKLNSVAI GAHWSCFIVL TITTFYLGYE SWTSRGPSKR
61: TSFYAGYQEE QNLALFVNFF AMLSYFGKIV ADTLGHNFGD VGPFIIGFGN YRYADYMLTC
121: PMLVYDLLYQ LRAPYRVSCS AIIFAILMSG VLAEFYAEGD PRLRNGAYAW YGFGCFWFIF
181: AYSIVMSIVA KQYSRLAQLA QDTGAEHSLH VLKFAVFTFS MLWILFPLVW AICPRGFGWI
241: DDNWTEVAHC VCDIVAKSCY GFALARFRKT YDEELFRLLE QLGHDEDEFQ KLELDMRLSS
301: NGERLRRLSL NSLEVLFQ