Sandbox Reserved 1756
From Proteopedia
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{{Sandbox_Reserved_BHall_F22}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_BHall_F22}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
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Ornithine Aminotransferase | Ornithine Aminotransferase | ||
| - | <StructureSection load='7T9Z' size='340' side='right' caption='OAT | + | |
| + | <StructureSection load='7T9Z' size='340' side='right' caption='OAT Enzyme' 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.<scene name='93/934000/Amino_acid_300-304/8'>Text To Be Displayed</scene> |
== Function of your protein == | == Function of your protein == | ||
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Homo sapiens is the organism from which the HOAT is derived | Homo sapiens is the organism from which the HOAT is derived | ||
| - | These enzymes are comprised of | + | These enzymes are comprised of substrates - L-Orn, GABA and AVA. By using the soaking method, the GABA structure was covalently attached to the PLP, as well as the AVA structure. Both structures were covalently attached to both the PLP and Catalytic Lys292. |
== Biological relevance and broader implications == | == Biological relevance and broader implications == | ||
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== Important amino acids== | == Important amino acids== | ||
<scene name='93/934000/Amino_acid_300-304/1'>Amino acids 300-304</scene> are an important parts of the ligands binding site <ref>PMID:35460691</ref>. | <scene name='93/934000/Amino_acid_300-304/1'>Amino acids 300-304</scene> are an important parts of the ligands binding site <ref>PMID:35460691</ref>. | ||
| + | <scene name='93/934000/Amino_acid_300-304/10'>Text To Be Displayed</scene> | ||
Hydrogen bonding - Val 143, Asp 263, Gly 142 | Hydrogen bonding - Val 143, Asp 263, Gly 142 | ||
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Covalent bonding - Lys 292 | Covalent bonding - Lys 292 | ||
| - | Salt bridge - Asp | + | Salt bridge - Asp 263 and Arg |
Pi-stacking - Phe 177 | Pi-stacking - Phe 177 | ||
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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. | ||
| - | + | Important <scene name='93/934000/Main_secondary_features/1'>main secondary features</scene> to stabilize the protein | |
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| + | Each C=O consists of two oxygen atoms that form hydrogen bonds, which stabilize the secondary structure. A polar amino acid residue is on the outside and a nonpolar amino acid is inside the alpha helix since non-polar amino acids do not react with water. Beta sheet runs in an antiparallel direction of non-polar and polar amino acids. | ||
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| + | <scene name='93/934000/Features_of_quaternary/1'> Homodimer is quaternary structure and HOAT cotains homodimer.</scene> | ||
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| + | <scene name='93/934000/Space_fill/1'>Space fill</scene> represent of how much of molecules have occupied at the active site. | ||
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| + | == Other important features == | ||
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| + | <scene name='93/934000/Aa_aromatic/1'>Aromatic rings</scene> plays a role important role in protein structure and ligand binding. Aromatic ring is important of protein interaction that allows pi stacking and acts as acceptor for hydrogen bonds. It is important for protein structure and ligand binding. | ||
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| + | <scene name='93/934000/Aa_polar/1'> | ||
| + | Polar amino acids</scene> is important part of protein structure. It is found usually on the outside of the alpha and beta that is because of its water-loving quality. It help to determine the 3-D structure and its specifically function. | ||
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| - | The beta sheet contains 1 of the 3 catalytic amino acids. | ||
Current revision
| This Sandbox is Reserved from November 4, 2022 through January 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 1755 through Sandbox Reserved 1764. |
To get started:
More help: Help:Editing |
Ornithine Aminotransferase
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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
- ↑ Butrin A, Butrin A, Wawrzak Z, Moran G, Liu D. Determination of the pH-Dependence, Substrate Specificity and Turnovers of Alternative Substrates for Human Ornithine Aminotransferase. J Biol Chem. 2022 Apr 20:101969. doi: 10.1016/j.jbc.2022.101969. PMID:35460691 doi:http://dx.doi.org/10.1016/j.jbc.2022.101969
