Sandbox Reserved 1757

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== Biological relevance and broader implications ==
== Biological relevance and broader implications ==
This article’s goal was to test the function and relation of the protein Mevalonate 3,5-bisphosphate and compare it to its homologs. The article seeks to explore the evolutionary changes that the protein has gone through that managed to separate it from its suspected evolutionary predecessors which require ATP to function and allowed it to become ATP-independent. This suspected evolutionary relevance is due to the residual signs of the ATP binding site which are still present in the Mevalonate 3,5-bisphosphate despite the protein being completely ATP-independent.
This article’s goal was to test the function and relation of the protein Mevalonate 3,5-bisphosphate and compare it to its homologs. The article seeks to explore the evolutionary changes that the protein has gone through that managed to separate it from its suspected evolutionary predecessors which require ATP to function and allowed it to become ATP-independent. This suspected evolutionary relevance is due to the residual signs of the ATP binding site which are still present in the Mevalonate 3,5-bisphosphate despite the protein being completely ATP-independent.
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[[Image:Oleic Acid.png|300 px|thumb|right|[Oleic Acid(suspected ligand present)]]]
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[[Image:Oleic Acid.png|300 px|thumb|right|Oleic Acid(suspected ligand present)]]
== Important amino acids==
== Important amino acids==
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Unfortunately due to the relatively recent studies pertaining to the structure and bind of Mevalonate 3,5-bisphosphate, the researchers are not exactly sure what the ligand present in the protein is. However, through this study, they determined that the closest match they could find for the <scene name='93/934001/Ligand_view/2'>ligand</scene> present is oleic acid. The ligand is bound via hydrogen bonding to H2O and <scene name='93/934001/Arg_128/2'>Arg 128</scene>. Another essential amino acid is the aspartate residue(<scene name='93/934001/Asp_309/1'>Asp309</scene>) as loss of this catalyst results in complete loss of Mevalonate 3,5-bisphosphate decarboxylase activity.
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Unfortunately due to the relatively recent studies pertaining to the structure and bind of Mevalonate 3,5-bisphosphate, the researchers are not exactly sure what the ligand present in the protein is. However, through this study, they determined that the closest match they could find for the <scene name='93/934001/Ligand_view/2'>ligand</scene> present is Oleic Acid(OLA). The ligand is bound via hydrogen bonding to H2O and <scene name='93/934001/Arg_128/2'>Arg 128</scene>. Another essential amino acid is the aspartate residue(<scene name='93/934001/Asp_309/1'>Asp309</scene>) as loss of this catalyst results in complete loss of Mevalonate 3,5-bisphosphate decarboxylase activity.
== Structural highlights ==
== Structural highlights ==
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Mevalonate 3,5-bisphosphate is a homodimer made up of <scene name='93/934001/Secondary/1'>40% alpha helices and 60% beta-sheets</scene>. Because Mevalonate 3,5-bisphosphate is a homodimer both molecules present are <scene name='93/934001/Quat/1'>identical</scene> in primary, secondary, and tertiary structure.
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The protein is a dimer that contains <scene name='93/934001/Secondary_structure/1'>14 helices and 15 beta sheets</scene> per linked molecule. The ARG 148 forms hydrogen bonds that allow it to pair with Oleic Acid, the protein’s ligand. Protein also requires H2O to be present in order to bind its <scene name='93/934001/Ligand/2'>ligand</scene>. I found it really interesting that the protein only actually attaches to the ligand via small interaction between ARG 128 and water molecules.
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Mevalonate 3,5-bisphosphate is amphipathic as showcased by the surplus of hydrophobic as well as hydrophilic amino acids present in its <scene name='93/934001/Active_site/2'>Active Site</scene>. This<scene name='93/934001/Active_site/4'> view</scene> also shows us the large cleft for substrate binding present on the molecule.
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</StructureSection>
</StructureSection>

Revision as of 16:28, 13 December 2022

This Sandbox is Reserved from November 4, 2022 through January 1, 2023 for use in the course CHEM 351 Biochemistry taught by Bonnie Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1755 through Sandbox Reserved 1764.
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Mevalonate 3,5-bisphosphate decarboxylase

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References 

 Aoki, M., Vinokur, J., Motoyama, K., Ishikawa, R., Collazo, M., Cascio, D., Sawaya, M. R., Ito, T., Bowie, J. U., & Hemmi, H. (2022). Crystal structure of mevalonate 3,5-bisphosphate decarboxylase reveals insight into the evolution of decarboxylases in the mevalonate metabolic pathways. The Journal of Biological Chemistry, 298(7), 102111–102111. https://doi.org/10.1016/j.jbc.2022.102111
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