Sandbox Reserved 1236
From Proteopedia
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==Luciferase== | ==Luciferase== | ||
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== Function == | == Function == | ||
| - | + | Luciferase | |
| - | + | Luciferase is an enzyme that catalyzes bioluminescence in the insect Photinus pyralis, more commonly known as fireflies. This protein causes the distinctive yellow flash seen in from the bottom of the insect. Photinus pyralis uses this protein in mate attraction, but enzyme is not unique to this one species and derivatives can be found many other organisms <ref>Conti, E., Franks, N. P., & Brick, P. (1996). Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure, 4(3), 287-298.</ref>. | |
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== Disease == | == Disease == | ||
== Relevance == | == Relevance == | ||
| - | + | This protein has been utilized in various types of assays to quantify the amount of ATP and to analyze the rate of transcription within a cell<ref>Wet, J. R., Wood, K. V., Helinski, D. R., & Deluca, M. (1985). Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli. Proceedings of the National Academy of Sciences, 82(23), 7870-7873. </ref>. This molecule is especially unique due to the fact that is very efficient in producing a photon through the reaction. It has potential for further biological applications in the future. | |
== Structural highlights == | == Structural highlights == | ||
| - | + | The structure of this protein comprises of two prominent domains. The larger one contains an N terminal distorted beta-barrel accompanied by alpha helices. The second and smaller unit is consist of a beta sheet and alpha helix complex <ref>Viviani, V. R. (2002). The origin, diversity, and structure function relationships of insect luciferases. Cellular and Molecular Life Sciences, 59(11), 1833-1850. </ref>. The process of fluorescence is achieved through a two-step oxidation reaction involving the substrate Lucinferin accompanied with ATP, Magnesium and oxygen. The first step consist of using ATP-Mg in an Acylation reaction of the COOH group on Lucinferin producing a Luciferyl adenylate intermediate and a phosphate group. The second reaction uses oxygen to create an excited state of the molecule. The molecule then returns to its ground state emitting a photon of light (Conti et al., 1996). A single peptide has been discover that plays a vital role in the photooxidation by Luciferase. The specific amino acid is a histidine located in the region 244HHGF247 of the protein <ref>Branchini, B. R., Magyar, R. A., Marcantonio, K. M., Newberry, K. J., Stroh, J. G., Hinz, L. K., & Murtiashaw, M. H. (1997). Identification of a Firefly Luciferase Active Site Peptide Using a Benzophenone-based Photooxidation Reagent. Journal of Biological Chemistry, 272(31), 19359-19364.</ref>. It has been shown to be necessary for the use of oxygen in the second part of the reaction. | |
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. | 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. | ||
Revision as of 20:59, 8 March 2017
| This Sandbox is Reserved from Jan 17 through June 31, 2017 for use in the course Biochemistry II taught by Jason Telford at the Maryville University, St. Louis, USA. This reservation includes Sandbox Reserved 1225 through Sandbox Reserved 1244. |
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Luciferase
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References
- ↑ Conti, E., Franks, N. P., & Brick, P. (1996). Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure, 4(3), 287-298.
- ↑ Wet, J. R., Wood, K. V., Helinski, D. R., & Deluca, M. (1985). Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli. Proceedings of the National Academy of Sciences, 82(23), 7870-7873.
- ↑ Viviani, V. R. (2002). The origin, diversity, and structure function relationships of insect luciferases. Cellular and Molecular Life Sciences, 59(11), 1833-1850.
- ↑ Branchini, B. R., Magyar, R. A., Marcantonio, K. M., Newberry, K. J., Stroh, J. G., Hinz, L. K., & Murtiashaw, M. H. (1997). Identification of a Firefly Luciferase Active Site Peptide Using a Benzophenone-based Photooxidation Reagent. Journal of Biological Chemistry, 272(31), 19359-19364.
