Sandbox Reserved 1804
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{{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_CHEM351_Spring2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
- | == | + | ==Beta-Propeller Protein== |
- | <StructureSection load=' | + | <StructureSection load='7RIS' size='340' side='right' caption='Beta-Propeller Protein' 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 == | ||
- | + | Transport protein that hydrolyzes aliphatic and aromatic lactones and esters. | |
+ | Is from Rhodopseudomonas palustris which is relevant because it prefers hydrophobic substances. | ||
== Biological relevance and broader implications == | == Biological relevance and broader implications == | ||
- | + | It has an X-ray structure and the secondary structure is also called a blade. It produces toroids of between four and twelve repeats which are almost always rearranged sequentially in a single peptide chain. Has three main ligands and those are phosphate ion, calcium ion and sodium ion. | |
== Important amino acids== | == Important amino acids== | ||
- | + | <scene name='95/954101/Amino_acids_300-304/2'>Amino Acids 300-304</scene> are an important part of the drug binding site <ref>PMID: 36502920</ref>. | |
- | + | <scene name='95/954101/Amino_acids_290-294/1'>Amino Acids 290-294</scene> are an important part of the drug binding site <ref>PMID:36502920</ref>. | |
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</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> |
Current revision
This Sandbox is Reserved from Mar 1 through Jun 1, 2023 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 1796 through Sandbox Reserved 1811. |
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Beta-Propeller Protein
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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
- ↑ Hall BW, Bingman CA, Fox BG, Noguera DR, Donohue TJ. A broad specificity beta-propeller enzyme from Rhodopseudomonas palustris that hydrolyzes many lactones including gamma-valerolactone. J Biol Chem. 2022 Dec 8:102782. doi: 10.1016/j.jbc.2022.102782. PMID:36502920 doi:http://dx.doi.org/10.1016/j.jbc.2022.102782
- ↑ Hall BW, Bingman CA, Fox BG, Noguera DR, Donohue TJ. A broad specificity beta-propeller enzyme from Rhodopseudomonas palustris that hydrolyzes many lactones including gamma-valerolactone. J Biol Chem. 2022 Dec 8:102782. doi: 10.1016/j.jbc.2022.102782. PMID:36502920 doi:http://dx.doi.org/10.1016/j.jbc.2022.102782