1xio

From Proteopedia

Revision as of 00:06, 25 November 2007

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 RET and PEE 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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