Bacteriorhodopsin: Difference between revisions

Latest revision as of 07:58, 8 August 2024

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. The retinal interacts predominantly with hydrophobic and aromatic residues ^[9] (Hydrophobic, Polar).

3D Structures of bacteriorhodopsin

Bacteriorhodopsin 3D structures

↑ 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:https://dx.doi.org/10.1126/science.aah3497
↑ 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
↑ 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:https://dx.doi.org/10.1016/j.tim.2006.09.005
↑ 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:https://dx.doi.org/10.1016/j.bbabio.2008.05.005
↑ 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:https://dx.doi.org/10.1016/j.celrep.2016.07.057
↑ 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:https://dx.doi.org/10.1016/j.bbabio.2013.09.010
↑ 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:https://dx.doi.org/10.1038/srep01635
↑ 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:https://dx.doi.org/10.1186/1745-6150-6-52
↑ 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

References

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Michal Harel, Alexander Berchansky, Wayne Decatur, Jaime Prilusky, Joel L. Sussman

[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:https://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:https://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:https://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:https://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:https://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:https://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:https://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

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@@ Line 1: / Line 1: @@
-{{STRUCTURE_1kg8|  PDB=1kg8  | SIZE=400| SCENE= |right|CAPTION=Bacteriorhodopsin complex with lipid and retinal, [[1kg8]] }}
+<StructureSection load='' size='350' side='right' scene='46/463242/Cv/4' caption='Bacteriorhodopsin complex with retinal, [[3han]]'>
+__TOC__
+== Function ==
-'''Bacteriorhodopsin''' (Br) is a membrane protein in Archaea which moves protons across the cell membrane.  Br is composed of 6 α-helical elements each containing a retinal molecule.  The retinal changes its conformation upon binding of a proton, causing the Br to change conformation and pump the proton.
+'''Bacteriorhodopsin''' (Br) is a membrane protein in Archaea which moves protons across the cell membrane<ref>PMID:28008064</ref>.  See also [[Bacteriorhodopsin (Hebrew)]].<br />
+'''Halorhodopsin''' uses light energy to pump chloride through biological membranes in Haloarchaea<ref>PMID:10827943</ref>.<br />
+'''Sensory rhodopsin''' uses light energy to pump calcium ions through biological membranes.  They are ubiquitous and use retinal as their chromophore<ref>PMID:17005405</ref>.<br />
+'''Xanthorhodopsin''' is a light-driven proton pump which uses the carotenoid salinixanthin as a second chromophore<ref>PMID:18515067</ref>.<br />
+'''Archaerhodopsin''' responds to yellow or green light by pumping protons out of cells and are used as optogenetic tools<ref>PMID:27524609</ref>.<br />
+'''Proteorhodopsins''' are the most abundant retinal-based photoreceptors.  It is found in many marine bacteria<ref>PMID:24060527</ref>.<br />
+'''Deltarhodopsin''' is a light-driven proton pump found in the archaebacteria ''Halloterrigena turkmenica''<ref>PMID:23567447</ref>.<br />
+'''Xenorhodopsin''' is an enigmatic new class of microbial rhodopsins<ref>PMID:21985229</ref>.<br />
-{{TOC limit|limit=2}}
+See also [[Rhodopsin]]
+== 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. <scene name='46/463242/Cv/6'>The retinal interacts predominantly with hydrophobic and aromatic residues</scene> <ref>PMID:19603754</ref> ({{Template:ColorKey_Hydrophobic}},  {{Template:ColorKey_Polar}}).
 == 3D Structures of bacteriorhodopsin ==
+[[Bacteriorhodopsin 3D structures]]
+</StructureSection>
+==See Also==
+*[[Rhodopsin]]
+*[[G protein-coupled receptor]]
+== References ==
+<references/>
+[[he:Bacteriorhodopsin_(Hebrew)]]
 [[Category:Topic Page]]

Bacteriorhodopsin: Difference between revisions

Latest revision as of 07:58, 8 August 2024

Contents

Function

Structural highlights

3D Structures of bacteriorhodopsin

See Also

References

Proteopedia Page Contributors and Editors (what is this?)

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