9h1x

Continuously illuminated structure of Sensory Rhodopsin II solved by serial millisecond crystallography

spinqualitylabelsall models 9h1x, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9h1x is a 1 chain structure with sequence from Natronomonas pharaonis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: CL, RET Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BACS2_NATPH Involved in the control of phototaxis. Seems to activate a methyl-accepting protein (HTR-II). Photoreceptor for blue light. Publication Abstract from PubMed Microbial rhodopsins form a diverse family of light-sensitive seven-transmembrane helix retinal proteins that function as active proton or ion pumps, passive light-gated ion channels, and photosensors. To understand how light-sensing in archaea is initiated by sensory rhodopsins, we perform serial synchrotron X-ray crystallography (SSX) studies of light induced conformational changes in sensory rhodopsin II (NpSRII) from the archaea Natronomonas pharaonis, both collecting time-resolved SSX data and collecting SSX data during continuous illumination. Comparing light-induced electron density changes in NpSRII with those reported for bacteriorhodopsin (bR) reveals several common light-induced structural perturbations. Unlike bR, however, helix G of NpSRII does not unwind near the conserved lysine residue to which retinal is covalently bound and therefore transient water molecule binding sites do not arise immediately to the cytoplasmic side of retinal. These structural differences prolong the duration of the NpSRII photocycle relative to bR, allowing time for the light-initiated sensory signal to be amplified. Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography.,Bosman R, Ortolani G, Ghosh S, James D, Norder P, Hammarin G, Ulfarsdottir TB, Ostojic L, Weinert T, Dworkowski F, Tomizaki T, Standfuss J, Branden G, Neutze R Nat Commun. 2025 Apr 11;16(1):3460. doi: 10.1038/s41467-025-58263-x. PMID:40216733 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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