1h68 | pdb_00001h68

sensory rhodopsin II

spinqualitylabelsall models 1h68, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1h68 is a 1 chain structure with sequence from Atcc 35678. The March 2002 RCSB PDB Molecule of the Month feature on Bacteriorhodopsin by David S. Goodsell is 10.2210/rcsb_pdb/mom_2002_3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Sensory rhodopsins (SRs) belong to a subfamily of heptahelical transmembrane proteins containing a retinal chromophore. These photoreceptors mediate the cascade of vision in animal eyes and phototaxis in archaebacteria and unicellular flagellated algae. Signal transduction by these photoreceptors occurs by means of transducer proteins. The two archaebacterial sensory rhodopsins SRI and SRII are coupled to the membrane-bound HtrI and HtrII transducer proteins. Activation of these proteins initiates phosphorylation cascades that modulate the flagellar motors, resulting in either attractant (SRI) or repellent (SRII) phototaxis. In addition, transducer-free SRI and SRII were shown to operate as proton pumps, analogous to bacteriorhodopsin. Here, we present the x-ray structure of SRII from Natronobacterium pharaonis (pSRII) at 2.1-A resolution, revealing a unique molecular architecture of the retinal-binding pocket. In particular, the structure of pSRII exhibits a largely unbent conformation of the retinal (as compared with bacteriorhodopsin and halorhodopsin), a hydroxyl group of Thr-204 in the vicinity of the Schiff base, and an outward orientation of the guanidinium group of Arg-72. Furthermore, the structure reveals a putative chloride ion that is coupled to the Schiff base by means of a hydrogen-bond network and a unique, positively charged surface patch for a probable interaction with HtrII. The high-resolution structure of pSRII provides a structural basis to elucidate the mechanisms of phototransduction and color tuning. X-ray structure of sensory rhodopsin II at 2.1-A resolution.,Royant A, Nollert P, Edman K, Neutze R, Landau EM, Pebay-Peyroula E, Navarro J Proc Natl Acad Sci U S A. 2001 Aug 28;98(18):10131-6. Epub 2001 Aug 14. PMID:11504917 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bacteriorhodopsin 3D structures Rhodopsin

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