Sandbox Reserved 1757
From Proteopedia
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[[Image:Oleic Acid.png|300 px|thumb|right|[Oleic Acid(suspected ligand present)]]] | [[Image:Oleic Acid.png|300 px|thumb|right|[Oleic Acid(suspected ligand present)]]] | ||
== Important amino acids== | == Important amino acids== | ||
- | 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 | + | 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. |
== Structural highlights == | == Structural highlights == | ||
- | 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 | + | 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. |
Revision as of 15:53, 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