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Hosaka, Toshiaki; Nomura, Takashi; Kubo, Minoru; Nakane, Takanori; Fangjia, Luo; Sekine, Shun-Ichi; Ito, Takuhiro; Murayama, Kazutaka; Ihara, Kentaro; Ehara, Haruhiko; Kashiwagi, Kazuhiro; Katsura, Kazushige; Akasaka, Ryogo; Hisano, Tamao; Tanaka, Tomoyuki; Tanaka, Rie; Arima, Toshi; Yamashita, Ayumi; Sugahara, Michihiro; Naitow, Hisashi; Matsuura, Yoshinori; Yoshizawa, Susumu; Tono, Kensuke; Owada, Shigeki; Nureki, Osamu; Kimura-Someya, Tomomi; Iwata, So; Nango, Eriko; Shirouzu, Mikako
Proceedings of the National Academy of Sciences - PNAS, 03/2022, Letnik: 119, Številka: 9Journal Article
Light-driven chloride-pumping rhodopsins actively transport anions, including various halide ions, across cell membranes. Recent studies using time-resolved serial femtosecond crystallography (TR-SFX) have uncovered the structural changes and ion transfer mechanisms in light-driven cation-pumping rhodopsins. However, the mechanism by which the conformational changes pump an anion to achieve unidirectional ion transport, from the extracellular side to the cytoplasmic side, in anion-pumping rhodopsins remains enigmatic. We have collected TR-SFX data of rhodopsin-3 (NM-R3), derived from a marine flavobacterium, at 10-µs and 1-ms time points after photoexcitation. Our structural analysis reveals the conformational alterations during ion transfer and after ion release. Movements of the retinal chromophore initially displace a conserved tryptophan to the cytoplasmic side of NM-R3, accompanied by a slight shift of the halide ion bound to the retinal. After ion release, the inward movements of helix C and helix G and the lateral displacements of the retinal block access to the extracellular side of NM-R3. Anomalous signal data have also been obtained from NM-R3 crystals containing iodide ions. The anomalous density maps provide insight into the halide binding site for ion transfer in NM-R3.
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in: SICRIS
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