Sandbox Reserved 1638
From Proteopedia
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SidA is from Aspergillus fumigatus and is a fungal disease drug target that is involved in the production of hydromate-containing siderophores, that are used by a pathogen to take iron. This protein affects the lungs and can be fatal in humans and animals. Because iron is the host organism, it is sequestered by the iron-building proteins which makes it a restricted nutrient for SidA. This is relevant because they are finding new information about configurational dynamics in flavin-dependent monooxygenases. We are using this to understand all of the different active sites and their conformations during the catalytic cycle. This results in the fine-tuning of inhibitor discovery efforts. | SidA is from Aspergillus fumigatus and is a fungal disease drug target that is involved in the production of hydromate-containing siderophores, that are used by a pathogen to take iron. This protein affects the lungs and can be fatal in humans and animals. Because iron is the host organism, it is sequestered by the iron-building proteins which makes it a restricted nutrient for SidA. This is relevant because they are finding new information about configurational dynamics in flavin-dependent monooxygenases. We are using this to understand all of the different active sites and their conformations during the catalytic cycle. This results in the fine-tuning of inhibitor discovery efforts. | ||
== Important amino acids == | == Important amino acids == | ||
| - | The important amino acids to pay attention to are Tyr324, Tyr276, Ser325, Asn323, and Asn275. Tyr324 is important because it moves over by 10A and shifts away from the active site. We have a triad which consists of Asn323, -FTyr324, and -Ser325. <scene name='86/861620/Protein_view_2_residues/1'>The important residues to pay attention to are 1-28</scene>. | + | The important amino acids to pay attention to are Tyr324, Tyr276, Ser325, Asn323, and Asn275. Tyr324 is important because it moves over by 10A and shifts away from the active site. We have a triad which consists of Asn323, -FTyr324, and -Ser325. <scene name='86/861620/Protein_view_2_residues/1'>The important residues to pay attention to are 1-28</scene>. This image attacked to residues shows the residue amino acids to pay attention to. Our ligands are displayed in the next section but we see how some are and aren't bound. |
== Structural highlights == | == Structural highlights == | ||
| - | <scene name='86/861620/Ligand_only/1'>Our structure has but also doesn't have ligands</scene>. The ligands it does have are NADPH and FAD and they're bound, just not to the substrate | + | <scene name='86/861620/Ligand_only/1'>Our structure has but also doesn't have ligands</scene>. The ligands it does have are NADPH and FAD and they're bound, just not to the substrate. There are 4 crystal structures formed. <scene name='86/861620/Secondary/1'>Our secondary structures are in orange and show the polypeptide chains in a helices.</scene> |
== Other important features == | == Other important features == | ||
Revision as of 02:14, 8 December 2020
| This Sandbox is Reserved from 09/18/2020 through 03/20/2021 for use in CHEM 351 Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, IA. This reservation includes Sandbox Reserved 1628 through Sandbox Reserved 1642. |
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References
- ↑ 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
- ↑ 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
