6gyh

Crystal structure of the light-driven proton pump Coccomyxa subellipsoidea Rhodopsin CsR

spinqualitylabelsall models 6gyh, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6gyh is a 1 chain structure with sequence from 'chlorella vulgaris' c-169. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CLR, OLB, RET Gene: COCSUDRAFT_42526 ('Chlorella vulgaris' C-169) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The light-driven proton pump Coccomyxa subellipsoidea rhodopsin (CsR) provides-because of its high expression in heterologous host cells-an opportunity to study active proton transport under controlled electrochemical conditions. In this study, solving crystal structure of CsR at 2.0-A resolution enabled us to identify distinct features of the membrane protein that determine ion transport directivity and voltage sensitivity. A specific hydrogen bond between the highly conserved Arg(83) and the nearby nonconserved tyrosine (Tyr(14)) guided our structure-based transformation of CsR into an operational light-gated proton channel (CySeR) that could potentially be used in optogenetic assays. Time-resolved electrophysiological and spectroscopic measurements distinguished pump currents from channel currents in a single protein and emphasized the necessity of Arg(83) mobility in CsR as a dynamic extracellular barrier to prevent passive conductance. Our findings reveal that molecular constraints that distinguish pump from channel currents are structurally more confined than was generally expected. This knowledge might enable the structure-based design of novel optogenetic tools, which derive from microbial pumps and are therefore ion specific. Design of a light-gated proton channel based on the crystal structure of Coccomyxa rhodopsin.,Fudim R, Szczepek M, Vierock J, Vogt A, Schmidt A, Kleinau G, Fischer P, Bartl F, Scheerer P, Hegemann P Sci Signal. 2019 Mar 19;12(573). pii: 12/573/eaav4203. doi:, 10.1126/scisignal.aav4203. PMID:30890657 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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