Sandbox Reserved 1733
From Proteopedia
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{{Sandbox_Reserved_Kim_Lane}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_Kim_Lane}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
| - | == | + | ==Structure== |
| - | + | Bacteriorhodopsin has a sequence that has 248 amino acids, including 3 sets of 7 alpha helices and 3 sets of 2 antiparallel beta strands. There are 3 domains but it does not have a motif. bR is a homotrimer with three subunits and has a C-3 symmetry. | |
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== Function == | == Function == | ||
Bacteriorhodopsin functions as a proton pump that transports H^+ across the gradient and is driven by green light. The protons are used to create ATP. It is a vital part of the bacteria. Once bacteriorhodopsin absorbs a photon, catalysis is triggered, causing a conformational shift from trans to cis, a release of a proton, and a transfer of a proton. The catalytic cycle includes 6 steps of isomerization, accessibility change, and ion transport. | Bacteriorhodopsin functions as a proton pump that transports H^+ across the gradient and is driven by green light. The protons are used to create ATP. It is a vital part of the bacteria. Once bacteriorhodopsin absorbs a photon, catalysis is triggered, causing a conformational shift from trans to cis, a release of a proton, and a transfer of a proton. The catalytic cycle includes 6 steps of isomerization, accessibility change, and ion transport. | ||
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Without bacteriorhodopsin, the light would not be converted into the energy that drives the proton pump, making it much harder for bacteria cells to produce the ATP needed to function normally. | Without bacteriorhodopsin, the light would not be converted into the energy that drives the proton pump, making it much harder for bacteria cells to produce the ATP needed to function normally. | ||
== Structural highlights == | == Structural highlights == | ||
| - | + | Aspartic Acids 96 and 85 play a very important role in the function of bacteriorhodopsin. When substituted into glutamine, less than 10% | |
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 01:46, 14 November 2022
| This Sandbox is Reserved from August 30, 2022 through May 31, 2023 for use in the course Biochemistry I taught by Kimberly Lane at the Radford University, Radford, VA, USA. This reservation includes Sandbox Reserved 1730 through Sandbox Reserved 1749. |
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Contents |
Structure
Bacteriorhodopsin has a sequence that has 248 amino acids, including 3 sets of 7 alpha helices and 3 sets of 2 antiparallel beta strands. There are 3 domains but it does not have a motif. bR is a homotrimer with three subunits and has a C-3 symmetry.
Function
Bacteriorhodopsin functions as a proton pump that transports H^+ across the gradient and is driven by green light. The protons are used to create ATP. It is a vital part of the bacteria. Once bacteriorhodopsin absorbs a photon, catalysis is triggered, causing a conformational shift from trans to cis, a release of a proton, and a transfer of a proton. The catalytic cycle includes 6 steps of isomerization, accessibility change, and ion transport.
Disease
Relevance
Without bacteriorhodopsin, the light would not be converted into the energy that drives the proton pump, making it much harder for bacteria cells to produce the ATP needed to function normally.
Structural highlights
Aspartic Acids 96 and 85 play a very important role in the function of bacteriorhodopsin. When substituted into glutamine, less than 10%
</StructureSection>
