Sandbox Reserved 1558

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== Structural highlights and structure-function relationships ==
== Structural highlights and structure-function relationships ==
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The <scene name='82/823082/Catalytic_triad/2'>Catalytic Triad</scene> of this protein is primarily made of the amino acids that are the main factor in catalysis. The 3 amino acids are Phe-59, Tyr101, and Lys-134. The <scene name='82/823082/Spacefill_whole_protein/1'>spacefill</scene> allows us to see the different binding sites for this protein, the binding sites are allosteric. The <scene name='82/823082/Colored_secondary/1'>Secondary structure</scene> is a fold of LsdA of a seven-bladed -propeller, typical of the carotenoid cleavage oxygenates (CCO's), which typically catalyze the oxidative cleavage of a double bond in carotenoids. The <scene name='82/823082/Hydrogen_bonding/1'>active site</scene> occurs at the center of the propeller and contains an Fe2+.
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The <scene name='82/823082/Catalytic_triad/2'>Catalytic Triad</scene> of this protein is primarily made of the amino acids that are the main factor in catalysis. The 3 amino acids are Phe-59, Tyr101, and Lys-134. The <scene name='82/823082/Colored_secondary/1'>Secondary structure</scene> is a fold of LsdA of a seven-bladed -propeller, typical of the carotenoid cleavage oxygenates (CCO's), which typically catalyze the oxidative cleavage of a double bond in carotenoids. The <scene name='82/823082/Hydrogen_bonding/1'>active site</scene> occurs at the center of the propeller and contains an Fe2+. The <scene name='82/823082/Hydrophobicity_whole_protein/1'>Hydrophobicity</scene> and <scene name='82/823082/Spacefill_whole_protein/1'>spacefill</scene> view of the ligand in the protein, shows that both hydrophilic and hydrophobic residues are important to the ligand in the binding site.The space fill view allows us to see the different binding sites for this protein, the binding sites are allosteric.
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The <scene name='82/823082/Hydrophobicity_whole_protein/1'>Hydrophobicity</scene> and <scene name='82/823082/Spacefill_whole_protein/1'>spacefill</scene> view of the ligand in the protein, shows that both hydrophilic and hydrophobic residues are important to the ligand in the binding site.
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Revision as of 01:36, 9 December 2019

This Sandbox is Reserved from Aug 26 through Dec 12, 2019 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 1556 through Sandbox Reserved 1575.
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Lignostilbene-α,β-dioxygenase A (LsdA) Catalyzation

Caption for this structure

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References

Kuatsjah, Eugene, et al. “Identification of Functionally Important Residues and Structural Features in a Bacterial Lignostilbene Dioxygenase.” Journal of Biological Chemistry, vol. 294, no. 35, 2019, pp. 12911–12920., doi:10.1074/jbc.ra119.009428.

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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