Sandbox Reserved 1759
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
The Protein is composed of alpha helix, beta sheet, and random coils. The protein consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The two subunits are homodimers, containing 9 alpha helix and 15 beta sheets each. The alpha helixes and beta sheets loop and fold to form a <scene name='93/934003/Tertiary_structure/1'>3D globular protein</scene>. The <scene name='93/934003/Space_filling/1'>space filling</scene> model helps to highlight the globular nature of the protein. Amphipathic.....In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well | The Protein is composed of alpha helix, beta sheet, and random coils. The protein consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The two subunits are homodimers, containing 9 alpha helix and 15 beta sheets each. The alpha helixes and beta sheets loop and fold to form a <scene name='93/934003/Tertiary_structure/1'>3D globular protein</scene>. The <scene name='93/934003/Space_filling/1'>space filling</scene> model helps to highlight the globular nature of the protein. Amphipathic.....In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well | ||
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| + | MBD is ATP-independent but evolves from the ATP-dependent , The MBD enzymes ligand binding site overlaps with the ATP binding site of its homologous enzyme, DMD. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 01:57, 12 December 2022
Mevalonate 3,5-Bisphosphate Decarboxylase Structure
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References
- ↑ Azami Y, Hattori A, Nishimura H, Kawaide H, Yoshimura T, Hemmi H. (R)-mevalonate 3-phosphate is an intermediate of the mevalonate pathway in Thermoplasma acidophilum. J Biol Chem. 2014 Jun 6;289(23):15957-67. doi: 10.1074/jbc.M114.562686. Epub 2014, Apr 22. PMID:24755225 doi:http://dx.doi.org/10.1074/jbc.M114.562686
