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7O8K

NmHR light state structure at 300 us after photoexcitation determined by serial femtosecond crystallography (with extrapolated, dark and light dataset)

Summary for 7O8K
Entry DOI10.2210/pdb7o8k/pdb
DescriptorChloride pumping rhodopsin, RETINAL, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (5 entities in total)
Functional Keywordschloride pump, rhodopsin, membrane protein
Biological sourceNonlabens marinus S1-08
Total number of polymer chains1
Total formula weight35397.33
Authors
Primary citationMous, S.,Gotthard, G.,Ehrenberg, D.,Sen, S.,Weinert, T.,Johnson, P.J.M.,James, D.,Nass, K.,Furrer, A.,Kekilli, D.,Ma, P.,Brunle, S.,Casadei, C.M.,Martiel, I.,Dworkowski, F.,Gashi, D.,Skopintsev, P.,Wranik, M.,Knopp, G.,Panepucci, E.,Panneels, V.,Cirelli, C.,Ozerov, D.,Schertler, G.F.X.,Wang, M.,Milne, C.,Standfuss, J.,Schapiro, I.,Heberle, J.,Nogly, P.
Dynamics and mechanism of a light-driven chloride pump.
Science, 375:845-851, 2022
Cited by
PubMed Abstract: Chloride transport by microbial rhodopsins is an essential process for which molecular details such as the mechanisms that convert light energy to drive ion pumping and ensure the unidirectionality of the transport have remained elusive. We combined time-resolved serial crystallography with time-resolved spectroscopy and multiscale simulations to elucidate the molecular mechanism of a chloride-pumping rhodopsin and the structural dynamics throughout the transport cycle. We traced transient anion-binding sites, obtained evidence for how light energy is used in the pumping mechanism, and identified steric and electrostatic molecular gates ensuring unidirectional transport. An interaction with the π-electron system of the retinal supports transient chloride ion binding across a major bottleneck in the transport pathway. These results allow us to propose key mechanistic features enabling finely controlled chloride transport across the cell membrane in this light-powered chloride ion pump.
PubMed: 35113649
DOI: 10.1126/science.abj6663
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

226707

건을2024-10-30부터공개중

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