Sandbox Reserved 1636

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== Function of your Protein ==
== Function of your Protein ==
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<ref>PMID:32723870</ref>
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my protein is <scene name='86/861618/Protein_view_2/5'>Flavin, it is found in fungus. it is sort of a co-enzyme and a receptor at the same time, and it helps grab metals. so, its job is to provide iron which is a critical nutrient used by fungus.
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since it acts as a receptor as well, it does interact with NADH. </scene>
== Biological relevance and broader implications ==
== Biological relevance and broader implications ==
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this journal article is explaining the role of flavin FAD and how fungi uses it in the redox reaction as it takes ornithine to hydroxyornithine in order to grab the iron needed, because the bioavailability of iron in the environment is extremely limited. <ref>PMID:32723870</ref>
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this journal article also discussed Aspergillosis, which is a condition in which Aspergillus fumigatus infects the lungs causing fatal mycoses in humans as well as animals resulting in about 200,000 cases per year, in humans only, and it cases death in about half of this number.
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So, it is really important to study this protein and understands the mechanism with which it works in order to fight the infection and discover a new anti-fungal drug that will work better for both humans and animals.
== Important amino acids ==
== Important amino acids ==
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the catalytic cycle is initiated by the binding of NADPH resulting a reduction of the FAD.
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The most important contributions to protein ligand interactions are H-bonds and lipophilic contacts. They are driven by enthalpy and entropy. Solvation and desolvation then, affects either of <scene name='86/861618/Protein_view_2/12'>the ligands</scene>. On the other hand, the protein binding site plays a big role in the binding process.
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Ans 323, Tyr 324, and Ser 325 are the key amino acids
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<scene name='86/861618/Protein_view_3/4'>hydrophobic interactions</scene><scene name='86/861618/Protein_view_3/4'>Text To Be Displayed</scene> are highlighted in green.
== Structural highlights ==
== Structural highlights ==
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secondary structure: Flavin consists of about <scene name='86/861618/Protein_view_4/2'>80% α-helices, 10% β-sheets and 10% of other structures</scene>. Flavin also has four domains.
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tertiary and Quaternary structures: <scene name='86/861618/Protein_view_5/1'>electrostatic interactions and the overall 3-D folding driven by interactions between the different R groups, which are shown in pink</scene>
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== Other important features ==
== Other important features ==
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flavin is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. this helps converting ornithine to hydroxy ornithine which Oh groups help hold the iron and grab it to the fungus. this reaction is where energy is transferred.
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Current revision

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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  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
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References

  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
  3. ↑ Campbell AC, Stiers KM, Martin Del Campo JS, Mehra-Chaudhary R, Sobrado P, Tanner JJ. Trapping conformational states of a flavin-dependent N-monooxygenase in crystallo reveals protein and flavin dynamics. J Biol Chem. 2020 Jul 28. pii: RA120.014750. doi: 10.1074/jbc.RA120.014750. PMID:32723870 doi:http://dx.doi.org/10.1074/jbc.RA120.014750
  4. ↑ Campbell AC, Stiers KM, Martin Del Campo JS, Mehra-Chaudhary R, Sobrado P, Tanner JJ. Trapping conformational states of a flavin-dependent N-monooxygenase in crystallo reveals protein and flavin dynamics. J Biol Chem. 2020 Jul 28. pii: RA120.014750. doi: 10.1074/jbc.RA120.014750. PMID:32723870 doi:http://dx.doi.org/10.1074/jbc.RA120.014750
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