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1xio
From Proteopedia
(New page: 200px<br /><applet load="1xio" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xio, resolution 2.000Å" /> '''Anabaena sensory rh...) |
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| - | [[Image:1xio.jpg|left|200px]]<br /><applet load="1xio" size=" | + | [[Image:1xio.jpg|left|200px]]<br /><applet load="1xio" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xio, resolution 2.000Å" /> | caption="1xio, resolution 2.000Å" /> | ||
'''Anabaena sensory rhodopsin'''<br /> | '''Anabaena sensory rhodopsin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Microbial sensory rhodopsins are a family of membrane-embedded | + | 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== | ==About this Structure== | ||
| - | 1XIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with RET and PEE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1XIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with <scene name='pdbligand=RET:'>RET</scene> and <scene name='pdbligand=PEE:'>PEE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XIO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: signaling protein]] | [[Category: signaling protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:10 2008'' |
Revision as of 13:55, 21 February 2008
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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. with and as ligands. 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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