Sandbox Reserved 1412
From Proteopedia
| Line 2: | Line 2: | ||
==Rhodopsin== | ==Rhodopsin== | ||
| - | Bacteriorhodopsin is found in Archaea | + | Bacteriorhodopsin is a photoreceptor protein found in Archaea. When in the presence of light energy and protons, the protein undergoes a conformational change and pumps protons out of the cell, creating an electrochemical gradient with a more negative intracellular environment <ref>PMID:24364740</ref>. |
| Line 9: | Line 9: | ||
== Structure == | == Structure == | ||
| - | The protein's main structure is <scene name='77/777732/Helices/1'>7 transmembrane alpha helices</scene | + | The protein's main structure is <scene name='77/777732/Helices/1'>7 transmembrane alpha helices</scene>. |
| - | <p>The <scene name='77/777732/Ligand_v2/1'>retinal</scene> is at the center of the protein and is bound to the alpha helices. In bacterial rhodopsin, the retinal functions as a proton pump by a conformation from all trans to cis-13. The<scene name='77/777732/Cis-13/1'> 13th carbon</scene> goes from cis to trans when the retinal is hit by light, and this change pumps protons out of the cell.</p> | + | <p>Light energy and protonation of the molecule leads to a complex system of isomerization that releases a proton outside of the membrane. The <scene name='77/777732/Ligand_v2/1'>retinal</scene> is at the center of the protein and is bound to the alpha helices. In bacterial rhodopsin, the retinal functions as a proton pump by a conformation from all trans to cis-13. The<scene name='77/777732/Cis-13/1'> 13th carbon</scene> goes from cis to trans when the retinal is hit by light, and this change pumps protons out of the cell <ref>PMID:24364740</ref>.</p> |
== Function == | == Function == | ||
| + | , where it reacts in the presence of light. | ||
This proton pump is used to create a gradient that can be used for things like ATP synthesis. | This proton pump is used to create a gradient that can be used for things like ATP synthesis. | ||
Revision as of 01:36, 14 February 2018
|
| This Sandbox is Reserved from January through July 31, 2018 for use in the course HLSC322: Principles of Genetics and Genomics taught by Genevieve Houston-Ludlam at the University of Maryland, College Park, USA. This reservation includes Sandbox Reserved 1311 through Sandbox Reserved 1430. |
To get started:
More help: Help:Editing |
Contents |
Rhodopsin
Bacteriorhodopsin is a photoreceptor protein found in Archaea. When in the presence of light energy and protons, the protein undergoes a conformational change and pumps protons out of the cell, creating an electrochemical gradient with a more negative intracellular environment [1].
Structure
The protein's main structure is .
Light energy and protonation of the molecule leads to a complex system of isomerization that releases a proton outside of the membrane. The is at the center of the protein and is bound to the alpha helices. In bacterial rhodopsin, the retinal functions as a proton pump by a conformation from all trans to cis-13. The goes from cis to trans when the retinal is hit by light, and this change pumps protons out of the cell [2].
Function
, where it reacts in the presence of light. This proton pump is used to create a gradient that can be used for things like ATP synthesis.
References
- ↑ Ernst OP, Lodowski DT, Elstner M, Hegemann P, Brown LS, Kandori H. Microbial and animal rhodopsins: structures, functions, and molecular mechanisms. Chem Rev. 2014 Jan 8;114(1):126-63. doi: 10.1021/cr4003769. Epub 2013 Dec 23. PMID:24364740 doi:http://dx.doi.org/10.1021/cr4003769
- ↑ Ernst OP, Lodowski DT, Elstner M, Hegemann P, Brown LS, Kandori H. Microbial and animal rhodopsins: structures, functions, and molecular mechanisms. Chem Rev. 2014 Jan 8;114(1):126-63. doi: 10.1021/cr4003769. Epub 2013 Dec 23. PMID:24364740 doi:http://dx.doi.org/10.1021/cr4003769
