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<StructureSection load='4diu' size='340' side='right' caption='Structural Model of Protein 4DIU' scene=''>
<StructureSection load='4diu' size='340' side='right' caption='Structural Model of Protein 4DIU' scene=''>
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<ref>DOI 10.1002/ijch.201300024</ref> <ref>PMID:21638687</ref>
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<ref>PMID:21638687</ref>
== Overview of Esterase ==
== Overview of Esterase ==
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== Proposed Function ==
== Proposed Function ==
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This protein has alpha/beta-hydrolase activity and is of the esterase family. The SPRITE, BLAST, InterPro, and Dali Search along with other bioinformatics analyses consistently matched with carboxylesterases and other esterase-like proteins. SPRITE provided proteins that had similar residues in the active site of the enzyme. Multiple of the matching proteins were esterases and had an RMSD value of <0.5. The RMSD value gives insight into how similar the overlapping sections for the unknown and known proteins are. A value of less than 2 is desired when choosing proteins for reference as a value closer to zero means less deviation between sites. SwissDock and Chimera allowed for protein-ligand docking studies. Many of the highlighted interactions were ester-containing ligands and others were susceptible to hydrolysis. The isolated protein was introduced to 10 mM p-nitrophenyl acetate in a buffer with a pH of 6. Enzyme activity was measured, and the data was consistent with other hydrolases.
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This protein has alpha/beta-hydrolase activity and is of the esterase family. The SPRITE, BLAST, InterPro, and Dali Search along with other bioinformatics analyses consistently matched with carboxylesterases and other esterase-like proteins. SPRITE provided proteins that had similar residues in the active site of the enzyme. Multiple of the matching proteins were esterases and had an RMSD value of <0.5. The RMSD value gives insight into how similar the overlapping sections for the unknown and known proteins are. A value of less than 2 is desired when choosing proteins for reference as a value closer to zero means less deviation between sites. SwissDock and Chimera allowed for protein-ligand docking studies. Many of the highlighted interactions were ester-containing ligands and others were susceptible to hydrolysis. The isolated protein was introduced to p-nitrophenyl acetate in a buffer with a pH of 6. Enzyme activity was measured via a change in absorbance at 405nm. PNP is a substrate that when hydrolyzed produces a colored product which will lead to the solution absorbing more at 405nm. <ref>https://doi.org/10.1186%2F1471-2180-12-27</ref>. The data collected was consistent with that of hydrolases in other studies.
[[Image:Enzymeactivity.jpeg]]
[[Image:Enzymeactivity.jpeg]]
== Structural highlights ==
== Structural highlights ==

Revision as of 22:40, 25 April 2024

Protein 4DIU: Structure, Function, and Significance in Biological Systems

The protein 4DIU has been identified and characterized as a potential esterase enzyme based on in-depth analyses including bioinformatics, molecular docking studies, and laboratory experiments. Online tools such as BLAST, Dali, and InterPro often matched 4DIU with carboxylesterases and other esterase-like proteins. This suggests that its function involves hydrolysis of esters. In part to data from Swiss Dock, 4DIU is predicted to have binding sites with an affinity to substrates such as acetate, butyrate, phosphate, proline, decanoate, and dodecanoate. The protein 4DIU was grown, harvested, and isolated in a laboratory. SDS-PAGE analysis was used to confirm the identity of the protein via molecular weight. Once identified the enzyme's activity on the substrate p-nitrophenyl acetate was measured. This substrate was chosen because many hydrolases have an affinity for it and can hydrolyze the substrate. It was determined that the 4DIU protein functions best at a pH of 6.

Structural Model of Protein 4DIU

Drag the structure with the mouse to rotate

References

  1. 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
  2. https://doi.org/10.1186%2F1471-2180-12-27
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