title: Crystal structure of the channelrhodopsin light-gated cation channel.
abstract: Channelrhodopsins (ChRs) are light-gated cation channels derived from algae that have shown experimental utility in optogenetics; for example, neurons expressing ChRs can be optically controlled with high temporal precision within systems as complex as freely moving mammals. Although ChRs have been broadly applied to neuroscience research, little is known about the molecular mechanisms by which these unusual and powerful proteins operate. Here we present the crystal structure of a ChR (a C1C2 chimaera between ChR1 and ChR2 from Chlamydomonas reinhardtii) at 2.3 Å resolution. The structure reveals the essential molecular architecture of ChRs, including the retinal-binding pocket and cation conduction pathway. This integration of structural and electrophysiological analyses provides insight into the molecular basis for the remarkable function of ChRs, and paves the way for the precise and principled design of ChR variants with novel properties.
authors.affiliation: Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.
authors.forename: Hideaki E
authors.initials: HE
authors.lastname: Kato
authors.forename: Feng
authors.initials: F
authors.lastname: Zhang
authors.forename: Ofer
authors.initials: O
authors.lastname: Yizhar
authors.forename: Charu
authors.initials: C
authors.lastname: Ramakrishnan
authors.forename: Tomohiro
authors.initials: T
authors.lastname: Nishizawa
authors.forename: Kunio
authors.initials: K
authors.lastname: Hirata
authors.forename: Jumpei
authors.initials: J
authors.lastname: Ito
authors.forename: Yusuke
authors.initials: Y
authors.lastname: Aita
authors.forename: Tomoya
authors.initials: T
authors.lastname: Tsukazaki
authors.forename: Shigehiko
authors.initials: S
authors.lastname: Hayashi
authors.forename: Peter
authors.initials: P
authors.lastname: Hegemann
authors.forename: Andrés D
authors.initials: AD
authors.lastname: Maturana
authors.forename: Ryuichiro
authors.initials: R
authors.lastname: Ishitani
authors.forename: Karl
authors.initials: K
authors.lastname: Deisseroth
authors.forename: Osamu
authors.initials: O
authors.lastname: Nureki
mesh_terms: D000818:Animals; D001436:Bacteriorhodopsins / Q000737:chemistry; D001665:Binding Sites; D002412:Cations / Q000378:metabolism*; D002417:Cattle; D016825:Chlamydomonas reinhardtii / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D015640:Ion Channel Gating / Q000528:radiation effects*; D007473:Ion Channels / Q000737:chemistry* / Q000235:genetics / Q000528:radiation effects; D008027:Light; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000528:radiation effects; D012172:Retinaldehyde / Q000378:metabolism; D012243:Rhodopsin / Q000737:chemistry* / Q000235:genetics / Q000528:radiation effects; D012545:Schiff Bases / Q000737:chemistry; D055672:Static Electricity
chemical_list: D002412:Cations; D007473:Ion Channels; D011993:Recombinant Fusion Proteins; D012545:Schiff Bases; D001436:Bacteriorhodopsins; D012243:Rhodopsin; D012172:Retinaldehyde