Sandbox Reserved 1695
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- | {{Sandbox_Reserved_BHall_F21}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | + | <scene name='89/892738/Hydrophobicity/1'>Text To Be Displayed</scene><scene name='89/892738/Space_fill_model/1'>Text To Be Displayed</scene><scene name='89/892738/Tertiary_structure/1'>Text To Be Displayed</scene><scene name='89/892738/Active_site/1'>Text To Be Displayed</scene><scene name='89/892738/7esm/4'>Text To Be Displayed</scene>{{Sandbox_Reserved_BHall_F21}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> |
- | == | + | ==L-rhamnose-alpha-1,4-D-glucuronate lyase== |
<StructureSection load='7ESM' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='7ESM' size='340' side='right' caption='Caption for this structure' scene=''> | ||
This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page '''Sandbox 1677'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
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== Function of your protein == | == Function of your protein == | ||
- | + | The enzyme is 7ESM from PDB. A crystal structure of a <scene name='89/892738/7esm/4'>L-rhamnose-alpha-1,4-D-glucuronate lyase</scene> from the fungi Fusarium oxysporum highlights the structure of the enzyme and its ligand (RAM 601). The main function of the enzyme is to lyse the L-rhamnose from the end caps of non-reducing ends of the Gum Arabic (GA) carbohydrate complex. By lysing the L-rhamnose, the structure of GA is able to be revealed which no one has been able to see the structure of GA before. The enzyme has one ligand of relevance, the RAM connected at the active site of the enzyme labeled Ligand RAM 601. | |
== Biological relevance and broader implications == | == Biological relevance and broader implications == | ||
- | + | Typically, the normal biological function of this enzyme is to be used in digestion of GA. Fusarium Oxysporum specifically uses GA as its only source of carbon. The enzyme is unrivaled by any other naturally made enzyme at lysing the L-rhamnose from Gum Arabic carbohydrate complexes. When it is purified and enough of it is created to saturate the substrate, it is capable of lysing up to 95% of all L-rhamnose from the GA complex. Its efficiency has important scientific implications, as it may provide a way for scientists to further study GA carbohydrate structures which has yet to be seen. | |
== Important amino acids== | == Important amino acids== | ||
+ | <scene name='89/892738/Ligand_ram_601/1'>Figure 1.11</scene> The alpha-L-rhamnopyranose is a ligand bound to the active site of the GA-specific L-rhamnose-alpha-1,4-D-glucaronate lyase (7ESM) complex. | ||
+ | <scene name='89/892738/Active_site/1'>Figure 1.12</scene> Here we can see the sctive site in which 8 amino acids work in conjunction with one another to bind to the alpha-L-rhamnose ligand. The Active site includes Tyr28, Gly86, His87, Tyr152, Arg222, Asn277, Gln278, and Arg333 labelled as the amino acid followed by the sequence number of the amino acid in reference to the protein. | ||
+ | |||
+ | Basically, these two images help illustrate the important features of the enzyme mainly the active site and the ligand. The Bond types are all hydrogen bound to the ligand. | ||
+ | == Structural Highlights == | ||
+ | <scene name='89/892738/Secondary_structure/1'>Secondary structure</scene> includes the anti-parallel beta-pleated sheets in blue and the alpha-helices are in green. | ||
+ | |||
+ | <scene name='89/892738/Tertiary_structure/1'>Tertiary structure</scene> reveals the enzymes 3D structure and displays the proteins almost cylindrical shape. | ||
+ | |||
+ | <scene name='89/892738/Space_fill_model/1'>Space fill model</scene> reveals that the structure of the protein is much more dense and also better illustrates where the ligand-binding site is. | ||
+ | |||
+ | <scene name='89/892738/Hydrophobicity/1'>Hydrophobic view</scene> shows the regions in red display hydrophobic characteristics and as you can see there is no clear pattern or order to the enzymes structure indicating it is in between hydrophobic and hydrophilic. | ||
+ | |||
+ | <scene name='89/892738/Ball_and_stick_1/1'>Ball and stick model 1</scene> shows the concentration of red oxygen molecules in the center of the enzyme. | ||
- | == | + | <scene name='89/892738/Ball_and_stick_2/1'> Ball and stick model 2</scene> shows the different charges of certain regions of the enzyme. Red negative and blue positive. |
+ | |||
+ | <scene name='89/892738/Ball_and_stick_3/1'>Ball and stick model 3</scene> is an image of a color coordination of amino acids in order of the protein and it flows pretty uniformly | ||
== Other important features == | == Other important features == | ||
+ | <scene name='89/892738/Feature_1/1'>Important feature 1</scene> includes an oligosaccharide chain which acts as an L-rhamnose stabilizer and links them together in a chain and assuming the function of the sugar chain is later used as an energy source for the fungi later. | ||
- | + | <scene name='89/892738/Feature_2/1'>Important feature 2</scene> includes the sodium ion and acetate ion that act as ligand stabilizers to the protein. They basically help with the strength of ligand-binding for the protein. | |
+ | Overall these structures are important in the metabolic uses of this protein and without them the enzymatic function of the protein may diminish as a result. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
- | <references/> | + | <references/> <ref>34303708</ref> |
Current revision
This Sandbox is Reserved from 10/01/2021 through 01/01//2022 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1690 through Sandbox Reserved 1699. |
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L-rhamnose-alpha-1,4-D-glucuronate lyase
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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