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@ARTICLE{Zabelskii:626502,
      author       = {Zabelskii, Dmitrii and Bukhdruker, Sergey and Bukhalovich,
                      Siarhei and Tsybrov, Fedor and Lamm, Gerrit H. U. and
                      Astashkin, Roman and Doroginin, Demid and Matveev, Grigory
                      and Sudarev, Vsevolod and Kuzmin, Alexander and Zinovev,
                      Egor and Vlasova, Anastasiia and Ryzhykau, Yury and
                      Ilyinsky, Nikolay and Gushchin, Ivan and Bourenkov, Gleb and
                      Alekseev, Alexey and Round, Adam and Wachtveitl, Josef and
                      Bamberg, Ernst and Gordeliy, Valentin},
      title        = {{I}on-conducting and gating molecular mechanisms of
                      channelrhodopsin revealed by true-atomic-resolution
                      structures of open and closed states},
      journal      = {Nature structural $\&$ molecular biology},
      volume       = {32},
      number       = {8},
      issn         = {1545-9993},
      address      = {London [u.a.]},
      publisher    = {Nature Publishing Group},
      reportid     = {PUBDB-2025-01455},
      pages        = {1347 - 1357},
      year         = {2025},
      note         = {Waiting for fulltext},
      abstract     = {Channelrhodopsins (ChRs) have emerged as major optogenetics
                      tools, particularly in neuroscience. Despite their
                      importance, the molecular mechanism of ChR opening remains
                      elusive. Moreover, all reported structures of ChRs
                      correspond to either a closed or an early intermediate state
                      and lack the necessary level of detail owing to the limited
                      resolution. Here we present the structures of the closed and
                      open states of a cation-conducting ChR, OLPVR1, from Organic
                      Lake phycodnavirus, belonging to the family of viral ChRs
                      solved at 1.1- and 1.3-Å resolution at physiologically
                      relevant pH conditions (pH 8.0). OLPVR1 was expressed in
                      Escherichia coli and crystallized using an in meso approach,
                      and the structures were solved by X-ray crystallography. We
                      also present the structure of the OLPVR1 protonated state at
                      acidic pH (pH 2.5) at 1.4-Å resolution. Together, these
                      three structures elucidate the molecular mechanisms of the
                      channel’s opening and permeability in detail. Extensive
                      functional studies support the proposed mechanisms. Channel
                      opening is controlled by isomerization of the retinal
                      cofactor, triggering protonation of proton acceptors and
                      deprotonation of proton donors located in the three gates of
                      the channel. The E51 residue in the core of the central gate
                      (similar to E90 of ChR2 from Chlamydomonas reinhardtii)
                      plays a key role in the opening of the channel. E51 flips
                      out of the gate and towards the proton acceptor D200 (D253
                      in ChR2 in C. reinhardtii), establishing a hydrogen bond
                      between them. Despite differences in subfamilies of ChRs,
                      they share a common gate–cavity architecture, suggesting
                      that they could have similar general gating mechanisms.
                      These results enabled us to design viral rhodopsin with
                      improved properties for optogenetic applications. The
                      structural data and mechanisms might also be helpful for
                      better understanding other ChRs and their engineering.},
      cin          = {EMBL-User / EMBL},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40205223},
      doi          = {10.1038/s41594-025-01488-7},
      url          = {https://bib-pubdb1.desy.de/record/626502},
}