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Sandbox Reserved 1085
From Proteopedia
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==Endoribonuclease III== | ==Endoribonuclease III== | ||
<StructureSection load='1O0W' size='420' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1O0W' size='420' side='right' caption='Caption for this structure' scene=''> | ||
| - | + | Endoribonuclease III is a class 1 RNase III hydrolase enzyme. In general its function, which seems to be universally conserved, is the binding to and cleavage of dsRNA. Endoribonuclease III appears to be crucial for an organisms ability to rapidly adapt to environmental changes through dsRNA processing and decay. | |
| + | Universally, it has been shown to mediate RNA turnover at the post-transcriptional level through processing rRNAs, tRNAs, some mRNAs, as well as non-coding dsRNAs. In microbes, RNase III has been shown that it also represses the synthesis of virulence factors (through the cleavage of foreign RNA.) <ref>Lioliou E, Sharma CM, Caldelari I, et al. Global Regulatory Functions of the Staphylococcus aureus Endoribonuclease III in Gene Expression. Hughes D, ed. PLoS Genetics. 2012;8(6):e1002782. doi:10.1371/journal.pgen.1002782</ref> | ||
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| + | In eukaryotes, RNase III has also been shown to generate microRNAs and siRNAs, which are central to gene regulation pathways. | ||
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. | ||
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GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The chromophore, responsible for the fluorescent properties of the protein, is buried inside the beta barrel as part of the central alpha helix passing through the barrel. The chromophore forms via spontaneous cyclization and oxidation of three residues in the central alpha helix: -Thr65 (or Ser65)-Tyr66-Gly67. This cyclization and oxidation creates the chromophore's five-membered ring via a new bond between the threonine and the glycine residues.[1] | GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The chromophore, responsible for the fluorescent properties of the protein, is buried inside the beta barrel as part of the central alpha helix passing through the barrel. The chromophore forms via spontaneous cyclization and oxidation of three residues in the central alpha helix: -Thr65 (or Ser65)-Tyr66-Gly67. This cyclization and oxidation creates the chromophore's five-membered ring via a new bond between the threonine and the glycine residues.[1] | ||
| - | + | == Structural highlights == | |
== Function == | == Function == | ||
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== Relevance == | == Relevance == | ||
| - | == Structural highlights == | ||
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. | ||
Revision as of 07:40, 22 April 2015
| This Sandbox is Reserved from 15/04/2015, through 15/06/2015 for use in the course "Protein structure, function and folding" taught by Taru Meri at the University of Helsinki. This reservation includes Sandbox Reserved 1081 through Sandbox Reserved 1090. |
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Endoribonuclease III
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References
- ↑ Lioliou E, Sharma CM, Caldelari I, et al. Global Regulatory Functions of the Staphylococcus aureus Endoribonuclease III in Gene Expression. Hughes D, ed. PLoS Genetics. 2012;8(6):e1002782. doi:10.1371/journal.pgen.1002782
- ↑ 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
