Sandbox Reserved 1635
From Proteopedia
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{{Sandbox_Reserved_BHall_F20}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_BHall_F20}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
- | == | + | ==Structure== |
- | <StructureSection load=' | + | <StructureSection load='6YSA' size='340' side='right' caption='Caption for this structure' scene=''> |
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
== Function of your Protein == | == Function of your Protein == | ||
- | + | Legumain Beta (6YSA) is a protein that helps with seed maturation and plant programmed cell death. <scene name='86/861617/Ligand_view/2'>Here has it binds with the ligand to help with it's functions</scene>. The protein is used in many of our medical advancements today. | |
== Biological relevance and broader implications == | == Biological relevance and broader implications == | ||
- | + | 6YSA is found in plants called, Arabidopsis thaliana. 6YSA is important because it's dual protease and ligase activity. These enzymes have become biotechnical interest. Their dual protease and ligase activites are still not well known about today. That this particular protein is heavily researched today. | |
== Important amino acids == | == Important amino acids == | ||
- | + | Important amino acids within this protein are asparagine, histidine, and cysteine. Most of the amino acids are bound together by hydrogen bonds. Amino acids form the catalytic residues that lower activation energy in an enzyme-catalyzed reaction <scene name='86/861617/Amino_acids/1'>Amino Acids</scene>. | |
== Structural highlights == | == Structural highlights == | ||
- | + | In the secondary structure, there are 10 alpha helices <scene name='86/861617/Secondary_structure/2'>Secondary Structure</scene>. The tertiary structure contains Citric Acid (CIT) and Sulfate Ion (SO4). There are many Hydrophobic Parts with this protein. <scene name='86/861617/Hydrophobic_parts/1'>Hydrophobic Parts</scene>. Most of the protein is hydrophobic which is all the purple parts. | |
== Other important features == | == Other important features == | ||
- | + | There are two main autocatalytic cleavage sites, Asn333 and Asn345. Upon incubation at pH ,5.0, you can observe additional cleavage sites on the LSAM domain, including Asp363, Asp416, and Asp417. This is important because it initiates Proteolytic Activation. Meaning it's breaking down the proteins into smaller polypeptides or amino acids. | |
- | + | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
+ | <ref>PMID:32719006</ref> |
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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Structure
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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