Sandbox Reserved 1733

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== References ==
== References ==
<references/>
<references/>
 +
Butt, H. J.; Fendler, K.; Bamberg, E.; Tittor, J.; Oesterhelt, D. Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump. EMBO. 1989, 8 (6), 1657-1663.
 +
 +
Edman, K.; Nollert, P.; Royant, A.; Belrhali, H.; Pebay-Peyroula, E.; Hajdu, J.; Neutze, R.; Landau, E. M. High resolution x-ray structure of an early intermediate in the bacteriorhodopsin photocycle. RSCB PDB. 1999, 401 (6755), 822-826.
 +
 +
Haupts, U.; Tittor, J.; Oesterhelt, D. Closing in on bacteriorhodopsin: progress in understanding the molecule. Annu. Rev. Biophys. Biomol. Struct. 1999, 28, 367-399.
 +
 +
Khorana, H. G.; Gerber, G. E.; Herlihy, W. C.; Gray, C. H.; Anderegg, R. J.; Nihei, K.; Biemann, K. Amino acid sequence of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 1997, 76 (10), 5046-5050.
 +
 +
Lanyi, J. K.; Varo, G. The photocycles of bacteriorhodopsin. Isr. J. Chem. 1995, 35 (3-4), 365-385.
 +
 +
Noort, J. Unraveling bacteriorhodopsin. Biophys. J. 2005, 88 (2), 763-764.
 +
 +
Ovchinnikov, Y. A.; Abdulaev, N. G.; Feigina, M. Y.; Kiselev, A. V.; Lobanov, N. A. The structural basis of the functioning of bacteriorhodopsin: an overview. ICHB. 1979, 100 (2), 219-224.
 +
 +
Ovichinnikov, Y. A.; Rhodopsin and bacteriorhodopsin structure--function relationships. IBCH. USSR 1982, 148 (2), 179-191.
 +
 +
Stoeckenius, W.; Bogomolni, R. A. Bacteriorhodopsin and related pigments of halobacteria. Ann. Rev. Biochem. 1982, 52, 587-616.
 +
 +
Wong, C. W.; Ko, L. N.; Huang, H. J.; Yang, C. S.; Hsu, S. H. Engineered bacteriorhodopsin may induce lung cancer cell cycle arrest and suppress their proliferation and migration. MDPI. 2021, 26 (23).

Revision as of 23:36, 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>

References

Butt, H. J.; Fendler, K.; Bamberg, E.; Tittor, J.; Oesterhelt, D. Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump. EMBO. 1989, 8 (6), 1657-1663.

Edman, K.; Nollert, P.; Royant, A.; Belrhali, H.; Pebay-Peyroula, E.; Hajdu, J.; Neutze, R.; Landau, E. M. High resolution x-ray structure of an early intermediate in the bacteriorhodopsin photocycle. RSCB PDB. 1999, 401 (6755), 822-826.

Haupts, U.; Tittor, J.; Oesterhelt, D. Closing in on bacteriorhodopsin: progress in understanding the molecule. Annu. Rev. Biophys. Biomol. Struct. 1999, 28, 367-399.

Khorana, H. G.; Gerber, G. E.; Herlihy, W. C.; Gray, C. H.; Anderegg, R. J.; Nihei, K.; Biemann, K. Amino acid sequence of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 1997, 76 (10), 5046-5050.

Lanyi, J. K.; Varo, G. The photocycles of bacteriorhodopsin. Isr. J. Chem. 1995, 35 (3-4), 365-385.

Noort, J. Unraveling bacteriorhodopsin. Biophys. J. 2005, 88 (2), 763-764.

Ovchinnikov, Y. A.; Abdulaev, N. G.; Feigina, M. Y.; Kiselev, A. V.; Lobanov, N. A. The structural basis of the functioning of bacteriorhodopsin: an overview. ICHB. 1979, 100 (2), 219-224.

Ovichinnikov, Y. A.; Rhodopsin and bacteriorhodopsin structure--function relationships. IBCH. USSR 1982, 148 (2), 179-191.

Stoeckenius, W.; Bogomolni, R. A. Bacteriorhodopsin and related pigments of halobacteria. Ann. Rev. Biochem. 1982, 52, 587-616.

Wong, C. W.; Ko, L. N.; Huang, H. J.; Yang, C. S.; Hsu, S. H. Engineered bacteriorhodopsin may induce lung cancer cell cycle arrest and suppress their proliferation and migration. MDPI. 2021, 26 (23).

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