Bacteriorhodopsin

From Proteopedia

Bacteriorhodopsin complex with retinal, 3han Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Structural highlights 3 3D Structures of bacteriorhodopsin Function Bacteriorhodopsin (Br) is a membrane protein in Archaea which moves protons across the cell membrane[1]. See also Bacteriorhodopsin (Hebrew). Halorhodopsin uses light energy to pump chloride through biological membranes in Haloarchaea[2]. Sensory rhodopsin uses light energy to pump calcium ions through biological membranes. They are ubiquitous and use retinal as their chromophore[3]. Xanthorhodopsin is a light-driven proton pump which uses the carotenoid salinixanthin as a second chromophore[4]. Archaerhodopsin responds to yellow or green light by pumping protons out of cells and are used as optogenetic tools[5]. Proteorhodopsins are the most abundant retinal-based photoreceptors. It is found in many marine bacteria[6]. Deltarhodopsin is a light-driven proton pump found in the archaebacteria Halloterrigena turkmenica[7]. Xenorhodopsin is an enigmatic new class of microbial rhodopsins[8]. Structural highlights Br is composed of 6 α-helical elements each containing a retinal molecule. The retinal changes its ground state conformation upon binding of a proton, causing the Br to change conformation to the activated state and pump the proton. [9] (Hydrophobic, Polar). 3D Structures of bacteriorhodopsin Bacteriorhodopsin 3D structures

See Also

• Rhodopsin
• G protein-coupled receptor

References

1. ↑ Nango E, Royant A, Kubo M, Nakane T, Wickstrand C, Kimura T, Tanaka T, Tono K, Song C, Tanaka R, Arima T, Yamashita A, Kobayashi J, Hosaka T, Mizohata E, Nogly P, Sugahara M, Nam D, Nomura T, Shimamura T, Im D, Fujiwara T, Yamanaka Y, Jeon B, Nishizawa T, Oda K, Fukuda M, Andersson R, Bath P, Dods R, Davidsson J, Matsuoka S, Kawatake S, Murata M, Nureki O, Owada S, Kameshima T, Hatsui T, Joti Y, Schertler G, Yabashi M, Bondar AN, Standfuss J, Neutze R, Iwata S. A three-dimensional movie of structural changes in bacteriorhodopsin. Science. 2016 Dec 23;354(6319):1552-1557. doi: 10.1126/science.aah3497. PMID:28008064 doi:http://dx.doi.org/10.1126/science.aah3497
2. ↑ Kolbe M, Besir H, Essen LO, Oesterhelt D. Structure of the light-driven chloride pump halorhodopsin at 1.8 A resolution. Science. 2000 May 26;288(5470):1390-6. PMID:10827943
3. ↑ Spudich JL. The multitalented microbial sensory rhodopsins. Trends Microbiol. 2006 Nov;14(11):480-7. doi: 10.1016/j.tim.2006.09.005. Epub, 2006 Sep 26. PMID:17005405 doi:http://dx.doi.org/10.1016/j.tim.2006.09.005
4. ↑ Lanyi JK, Balashov SP. Xanthorhodopsin: a bacteriorhodopsin-like proton pump with a carotenoid antenna. Biochim Biophys Acta. 2008 Jul-Aug;1777(7-8):684-8. doi:, 10.1016/j.bbabio.2008.05.005. Epub 2008 May 16. PMID:18515067 doi:http://dx.doi.org/10.1016/j.bbabio.2008.05.005
5. ↑ El-Gaby M, Zhang Y, Wolf K, Schwiening CJ, Paulsen O, Shipton OA. Archaerhodopsin Selectively and Reversibly Silences Synaptic Transmission through Altered pH. Cell Rep. 2016 Aug 23;16(8):2259-2268. doi: 10.1016/j.celrep.2016.07.057. Epub, 2016 Aug 11. PMID:27524609 doi:http://dx.doi.org/10.1016/j.celrep.2016.07.057
6. ↑ Bamann C, Bamberg E, Wachtveitl J, Glaubitz C. Proteorhodopsin. Biochim Biophys Acta. 2014 May;1837(5):614-25. doi: 10.1016/j.bbabio.2013.09.010., Epub 2013 Sep 20. PMID:24060527 doi:http://dx.doi.org/10.1016/j.bbabio.2013.09.010
7. ↑ Hara KY, Wada T, Kino K, Asahi T, Sawamura N. Construction of photoenergetic mitochondria in cultured mammalian cells. Sci Rep. 2013;3:1635. doi: 10.1038/srep01635. PMID:23567447 doi:http://dx.doi.org/10.1038/srep01635
8. ↑ Ugalde JA, Podell S, Narasingarao P, Allen EE. Xenorhodopsins, an enigmatic new class of microbial rhodopsins horizontally transferred between archaea and bacteria. Biol Direct. 2011 Oct 10;6:52. doi: 10.1186/1745-6150-6-52. PMID:21985229 doi:http://dx.doi.org/10.1186/1745-6150-6-52
9. ↑ Joh NH, Oberai A, Yang D, Whitelegge JP, Bowie JU. Similar energetic contributions of packing in the core of membrane and water-soluble proteins. J Am Chem Soc. 2009 Aug 12;131(31):10846-7. PMID:19603754 doi:10.1021/ja904711k