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Results 1 - 10
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35
Sy m posi um-i n-Pri nt: P hotoreceptors Evolutionary Patterns of Retinal-Binding Pockets of
"... Genome sequencing projects resulted in the identification of a large number of new sequence homologs of archaeal rhodopsins in marine bacteria, fungi, and unicellular algae. It is an important task to unambiguously predict the functions of these new rhodopsins, as it is difficult to perform individu ..."
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the retinal-binding pockets in high-resolution structures of rhodopsins and to extract residues forming the wall of the retinal-binding pocket. We then obtain a tree defining the functional relationship of rhodopsins based on the short sequences of residues forming the wall of the retinal-binding pocket
their functions
"... patterns of retinal-binding pockets of type I rhodopsins and ..."
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patterns of retinal-binding pockets of type I rhodopsins and
Dual Roles of DMPC and CHAPS in the Refolding of Bacterial Opsins In Vitro'
, 1996
"... The bacterial opsins can be refolded to regenerate the chromophore by transfer from SDS to DMPC/CHAPS/SDS mixed micelles in the presence of retinal. A sequential refolding model has been proposed for bacterioopsin [Booth et al. (1995) Nature Struct Biol. 2,139-143]. However, the roles of DMPC and CH ..."
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and CHAPS in the refolding process are not clear. In this study we measured the effects of DMPC and CHAPS on the refolding of bacterial opsins in vitro by CD and fluorescence spectroscopy. In contrast to in experiments in the presence of large amounts of DMPC, the process of retinal binding pocket formation
Mutagenesis studies of rhodopsin phototransduction
"... We employ the vertebrate visual proteins rhodopsin and transducin as a model system forstructure-function studies on the molecular mechanisms of transmembrane signaling. These visual proteins are members of a super-family of related guanine nucleotide-binding regulatory proteins (G proteins) and 0 p ..."
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protein-coupled receptors. We are particularly interested in the structures of the retinal binding pockets of visual pigments and in identifying the structural domains of both rhodopsin andtransducin involved in the G protein activation process.
11-cis-Retinal Protonated Schiff Base: The Effect of Environment and Solvent on the Chromophore of Rhodopsin
"... Recently the structure of rhodopsin was determined from the X-ray di#raction data extending to the resolution of 2.8 A. We have studied the e#ects of amino acids and of water using A density functional based tight-binding code. A model retinal binding pocket was employed containing 27 residues withi ..."
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Recently the structure of rhodopsin was determined from the X-ray di#raction data extending to the resolution of 2.8 A. We have studied the e#ects of amino acids and of water using A density functional based tight-binding code. A model retinal binding pocket was employed containing 27 residues
RESEARCH ARTICLE Crystal Structure of Escherichia coli- Expressed Haloarcula marismortui Bacteriorhodopsin I
"... . These authors contributed equally to this work. Bacteriorhodopsins are a large family of seven-helical transmembrane proteins that function as light-driven proton pumps. Here, we present the crystal structure of a new member of the family, Haloarcula marismortui bacteriorhodopsin I (HmBRI) D94N mu ..."
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mutant, at the resolution of 2.5 Å. While the HmBRI retinal-binding pocket and proton donor site are similar to those of other archaeal proton pumps, its proton release region is extended and contains additional water molecules. The protein’s fold is reinforced by three novel inter-helical hydrogen
Review Structural basis for sensory rhodopsin function
, 2002
"... The crystal structure of sensory rhodopsin II from Natronobacterium pharaonis was recently solved at 2.1 A ̊ resolution from lipidic cubic phase-grown crystals. A critical analysis of previous structure–function studies is possible within the framework of the high-resolution structure of this photor ..."
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of the retinal binding pocket is compact, representing a major determinant for the selective binding of the chromophore, all-trans retinal to the apoprotein, opsin. Several chromophore–protein interactions revealed by the structure were not predicted by previous mutagenesis and spectroscopic analyses
2 3 4 5 6 7 8
"... *Corresponding authors We have determined the structure of bovine rhodopsin at 2.65 A ˚ resolution using untwinned native crystals in the space group P31, by molecular replacement from the 2.8 A ˚ model (1F88) solved in space group P41. The new structure reveals mechanistically important details unr ..."
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unresolved previously, which are considered in the membrane context by docking the structure into a cryo-EM map of 2D crystals. Kinks in the transmembrane helices facilitate inter-helical polar interactions. Ordered water molecules extend the hydrogen bonding networks, linking Trp265 in the retinal binding
Picosecond Multidimensional Fluorescence Spectroscopy: A Tool to Measure Real-time Protein Dynamics During Function †
"... ABSTRACT Advanced multidimensional time-correlated single photon counting (mdTCSPC) and picosecond time-resolved fluorescence in combination with site-directed fluorescence labeling are valuable tools to study the properties of membrane protein surface segments on the pico-to nanoseconds time scale ..."
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two transitions between three intermediate states in the second part of the bR photocycle. Correlation with photocycle kinetics allows for the determination of reaction intermediates at the proteins surface which are coupled to changes in the retinal binding pocket.
A Ligand Channel through the G Protein Coupled Receptor Opsin
"... The G protein coupled receptor rhodopsin contains a pocket within its seven-transmembrane helix (TM) structure, which bears the inactivating 11-cis-retinal bound by a protonated Schiff-base to Lys296 in TM7. Light-induced 11-cis-/all-transisomerization leads to the Schiff-base deprotonated active Me ..."
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openings and comprises in its central part the retinal binding pocket. The channel traverses the receptor over a distance of ca. 70 A ˚ and is between 11.6 and 3.2 A ˚ wide. Both openings are lined with aromatic residues, while the central part is highly polar. Four constrictions within the channel are so
Results 1 - 10
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35
