Abstract
Channelrhodopsins (ChRs) are light-gated cation channels that mediate ion transport across membranes in microalgae (vectorial catalysis). ChRs are now widely used for the analysis of neural networks in tissues and living animals with light (optogenetics). For elucidation of functional mechanisms at the atomic level, as well as for further engineering and application, a detailed structure is urgently needed. In the absence of an experimental structure, here we develop a structural ChR model based on several molecular computational approaches, capitalizing on characteristic patterns in amino acid sequences of ChR1, ChR2, Volvox ChRs, Mesostigma ChR, and the recently identified ChR of the halophilic alga Dunaliella salina. In the present model, we identify remarkable structural motifs that may explain fundamental electrophysiological properties of ChR2, ChR1, and their mutants, and in a crucial validation of the model, we successfully reproduce the excitation energy predicted by absorption spectra.
| Original language | English |
|---|---|
| Pages (from-to) | 7456-7466 |
| Number of pages | 11 |
| Journal | Journal of Biological Chemistry |
| Volume | 287 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - 2012 Mar 2 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
Structural model of channelrhodopsin. / Watanabe, Hiroshi; Welke, Kai; Schneider, Franziska; Tsunoda, Satoshi; Zhang, Feng; Deisseroth, Karl; Hegemann, Peter; Elstner, Marcus.
In: Journal of Biological Chemistry, Vol. 287, No. 10, 02.03.2012, p. 7456-7466.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structural model of channelrhodopsin
AU - Watanabe, Hiroshi
AU - Welke, Kai
AU - Schneider, Franziska
AU - Tsunoda, Satoshi
AU - Zhang, Feng
AU - Deisseroth, Karl
AU - Hegemann, Peter
AU - Elstner, Marcus
PY - 2012/3/2
Y1 - 2012/3/2
N2 - Channelrhodopsins (ChRs) are light-gated cation channels that mediate ion transport across membranes in microalgae (vectorial catalysis). ChRs are now widely used for the analysis of neural networks in tissues and living animals with light (optogenetics). For elucidation of functional mechanisms at the atomic level, as well as for further engineering and application, a detailed structure is urgently needed. In the absence of an experimental structure, here we develop a structural ChR model based on several molecular computational approaches, capitalizing on characteristic patterns in amino acid sequences of ChR1, ChR2, Volvox ChRs, Mesostigma ChR, and the recently identified ChR of the halophilic alga Dunaliella salina. In the present model, we identify remarkable structural motifs that may explain fundamental electrophysiological properties of ChR2, ChR1, and their mutants, and in a crucial validation of the model, we successfully reproduce the excitation energy predicted by absorption spectra.
AB - Channelrhodopsins (ChRs) are light-gated cation channels that mediate ion transport across membranes in microalgae (vectorial catalysis). ChRs are now widely used for the analysis of neural networks in tissues and living animals with light (optogenetics). For elucidation of functional mechanisms at the atomic level, as well as for further engineering and application, a detailed structure is urgently needed. In the absence of an experimental structure, here we develop a structural ChR model based on several molecular computational approaches, capitalizing on characteristic patterns in amino acid sequences of ChR1, ChR2, Volvox ChRs, Mesostigma ChR, and the recently identified ChR of the halophilic alga Dunaliella salina. In the present model, we identify remarkable structural motifs that may explain fundamental electrophysiological properties of ChR2, ChR1, and their mutants, and in a crucial validation of the model, we successfully reproduce the excitation energy predicted by absorption spectra.
UR - http://www.scopus.com/inward/record.url?scp=84863229159&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84863229159&partnerID=8YFLogxK
U2 - 10.1074/jbc.M111.320309
DO - 10.1074/jbc.M111.320309
M3 - Article
C2 - 22241469
AN - SCOPUS:84863229159
VL - 287
SP - 7456
EP - 7466
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 10
ER -