TY  - JOUR
A1  - Müller, Maria
A1  - Bamann, Christian
A1  - Bamberg, Ernst
A1  - Kühlbrandt, Werner
T1  - Light-induced helix movements in channelrhodopsin-2
T2  - Journal of molecular biology
N2  - Channelrhodopsin-2 (ChR2) is a cation-selective light-gated channel from Chlamydomonas reinhardtii (Nagel G, Szellas T, Huhn W, Kateriya S, Adeishvili N, Berthold P, et al. Channelrhodopsin-2, a directly light-gated cation-selective membrane channel. Proc Natl Acad Sci USA 2003;100:13940-5), which has become a powerful tool in optogenetics. Two-dimensional crystals of the slow photocycling C128T ChR2 mutant were exposed to 473 nm light and rapidly frozen to trap the open state. Projection difference maps at 6Å resolution show the location, extent and direction of light-induced conformational changes in ChR2 during the transition from the closed state to the ion-conducting open state. Difference peaks indicate that transmembrane helices (TMHs) TMH2, TMH6 and TMH7 reorient or rearrange during the photocycle. No major differences were found near TMH3 and TMH4 at the dimer interface. While conformational changes in TMH6 and TMH7 are known from other microbial-type rhodopsins, our results indicate that TMH2 has a key role in light-induced channel opening and closing in ChR2.
KW  - channelrhodopsin
KW  - conformational changes
KW  - electron cryo-microscopy
KW  - light-gated ion channel
KW  - microbial rhodopsin
Y1  - 2014
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/37218
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-372187
SN  - 1089-8638
SN  - 0022-2836
N1  - © 2014 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by/3.0/).
VL  - 427
IS  - 2
SP  - 341
EP  - 349
PB  - Elsevier
CY  - Amsterdam [u.a.]
ER  -