Sandbox Reserved 1467
From Proteopedia
(Difference between revisions)
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{{Sandbox_Reserved_BHall_1}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_BHall_1}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
| - | == | + | ==Your Heading Here (maybe something like 'Structure')== |
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' 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. | ||
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== Relevance == | == Relevance == | ||
By studying the two mono-functional enzymes, ObcA and ObcB, there is a better understanding of the underlying molecular basis. A bifunctional enzyme, Obc 1, can be used here for oxalogenesis. Researching and finding out more about these enzymes can help advance knowledge and potentially develop ways to control diseases associated with the ''Burkholderia'' species. | By studying the two mono-functional enzymes, ObcA and ObcB, there is a better understanding of the underlying molecular basis. A bifunctional enzyme, Obc 1, can be used here for oxalogenesis. Researching and finding out more about these enzymes can help advance knowledge and potentially develop ways to control diseases associated with the ''Burkholderia'' species. | ||
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== Structural highlights == | == Structural highlights == | ||
The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices, with some additional beta sheets. | The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices, with some additional beta sheets. | ||
The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, N-domain (navy) and C-Domain (gray). The two domains in this protein, Obc1, mediate oxalogenesis. The N-domain consists of an ObcB activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses. | The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, N-domain (navy) and C-Domain (gray). The two domains in this protein, Obc1, mediate oxalogenesis. The N-domain consists of an ObcB activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses. | ||
| - | When looking at the <scene name='79/799595/Space_fill/1'>space-filling view of structure </scene> it is hard to distinguish between the different parts of the protein. This view, can give a better insight on the size, shape, and representation of the complete molecule. The <scene name='79/799595/Hydrophobic/1' | + | When looking at the <scene name='79/799595/Space_fill/1'>space-filling view of structure </scene> it is hard to distinguish between the different parts of the protein. This view, can give a better insight on the size, shape, and representation of the complete molecule. |
| + | The protein seems to be <scene name='79/799595/Hydrophobic/1'>equal parts</scene> hydrophobic and hydrophilic. | ||
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Ligand: | Ligand: | ||
<scene name='79/799595/Ligand/1'>Ligand</scene> | <scene name='79/799595/Ligand/1'>Ligand</scene> | ||
| - | Ser-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/1'> | + | Ser-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/1'>Catalytic Triad</scene> |
The catalytic triad is located in the C-domain is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein. | The catalytic triad is located in the C-domain is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein. | ||
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The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935. | The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935. | ||
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</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 00:57, 15 November 2018
| This Sandbox is Reserved from October 22, 2018 through April 30, 2019 for use in the course Biochemistry taught by Bonnie Hall at the Grand View University, Des Moines, IA USA. This reservation includes Sandbox Reserved 1456 through Sandbox Reserved 1470. |
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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
