1xio
From Proteopedia
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- | [[Image:1xio.jpg|left|200px]] | + | [[Image:1xio.jpg|left|200px]] |
- | + | ||
- | '''Anabaena sensory rhodopsin''' | + | {{Structure |
+ | |PDB= 1xio |SIZE=350|CAPTION= <scene name='initialview01'>1xio</scene>, resolution 2.000Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=RET:RETINAL'>RET</scene> and <scene name='pdbligand=PEE:PHOSPHATIDYLETHANOLAMINE'>PEE</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Anabaena sensory rhodopsin''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1XIO is a [ | + | 1XIO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XIO OCA]. |
==Reference== | ==Reference== | ||
- | Anabaena sensory rhodopsin: a photochromic color sensor at 2.0 A., Vogeley L, Sineshchekov OA, Trivedi VD, Sasaki J, Spudich JL, Luecke H, Science. 2004 Nov 19;306(5700):1390-3. Epub 2004 Sep 30. PMID:[http:// | + | Anabaena sensory rhodopsin: a photochromic color sensor at 2.0 A., Vogeley L, Sineshchekov OA, Trivedi VD, Sasaki J, Spudich JL, Luecke H, Science. 2004 Nov 19;306(5700):1390-3. Epub 2004 Sep 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15459346 15459346] |
[[Category: Anabaena sp.]] | [[Category: Anabaena sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signaling protein]] | [[Category: signaling protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:10:26 2008'' |
Revision as of 13:10, 20 March 2008
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, resolution 2.000Å | |||||||
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Ligands: | and | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Anabaena sensory rhodopsin
Overview
Microbial sensory rhodopsins are a family of membrane-embedded photoreceptors in prokaryotic and eukaryotic organisms. Structures of archaeal rhodopsins, which function as light-driven ion pumps or photosensors, have been reported. We present the structure of a eubacterial rhodopsin, which differs from those of previously characterized archaeal rhodopsins in its chromophore and cytoplasmic-side portions. Anabaena sensory rhodopsin exhibits light-induced interconversion between stable 13-cis and all-trans states of the retinylidene protein. The ratio of its cis and trans chromophore forms depends on the wavelength of illumination, thus providing a mechanism for a single protein to signal the color of light, for example, to regulate color-sensitive processes such as chromatic adaptation in photosynthesis. Its cytoplasmic half channel, highly hydrophobic in the archaeal rhodopsins, contains numerous hydrophilic residues networked by water molecules, providing a connection from the photoactive site to the cytoplasmic surface believed to interact with the receptor's soluble 14-kilodalton transducer.
About this Structure
1XIO is a Single protein structure of sequence from Anabaena sp.. Full crystallographic information is available from OCA.
Reference
Anabaena sensory rhodopsin: a photochromic color sensor at 2.0 A., Vogeley L, Sineshchekov OA, Trivedi VD, Sasaki J, Spudich JL, Luecke H, Science. 2004 Nov 19;306(5700):1390-3. Epub 2004 Sep 30. PMID:15459346
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