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==Rhodopsin== | ==Rhodopsin== | ||
| - | Bacteriorhodopsin is found in | + | Bacteriorhodopsin is found in Archaea, where it reacts in the presence of light. When hit by light and bound to a proton, the protein undergoes a conformational change and pumps protons out of the cell, creating an electrochemical gradient. |
| - | The protein has <scene name='77/777732/Helices/1'>7 transmembrane alpha helices</scene>. | ||
| - | <p><scene name='77/777732/Ligand_v2/1'>The 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> | ||
| - | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| + | == Structure == | ||
| + | |||
| + | The protein's main structure is <scene name='77/777732/Helices/1'>7 transmembrane alpha helices</scene> <ref>PMID:24364740</ref>. | ||
| + | |||
| + | <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> | ||
== Function == | == Function == | ||
| - | + | This proton pump is used to create a gradient that can be used for things like ATP synthesis. | |
| + | |||
| + | |||
| - | == Relevance == | ||
| - | == Structural highlights == | ||
| - | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
| - | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 01:21, 14 February 2018
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| 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. |
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Contents |
Rhodopsin
Bacteriorhodopsin is found in Archaea, where it reacts in the presence of light. When hit by light and bound to a proton, the protein undergoes a conformational change and pumps protons out of the cell, creating an electrochemical gradient.
Structure
The protein's main structure is [1].
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.
Function
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
