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From Proteopedia
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Aconitase is an enzyme participating in the citric acid cycle. It is highly conserved among many species. | Aconitase is an enzyme participating in the citric acid cycle. It is highly conserved among many species. | ||
| - | It has been shown <ref> pmid 15975908 </ref> that in yeast it is dually located in mitochondria and the cytosol by means of reverse translocation. To understand the underlying mechanism that enables this unique phenomena, a structural predicted model has been created using the I-TASSER homology modelling server <ref> pmid 18215316 </ref> | + | It has been shown <ref> pmid 15975908 </ref> that in yeast it is dually located in mitochondria and the cytosol by means of reverse translocation. To understand the underlying mechanism that enables this unique phenomena, a structural predicted model has been created using the I-TASSER homology modelling server <ref> pmid 18215316 </ref> <scene name='Sandbox_orly/Helices/1'>Bovine aconitase</scene> was used as the main template for this modelling. |
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Since prior experiments show that the last six residues are crucial for its dual targeting <ref> PMID 21440554 </ref>, a structural comparison has been performed looking at the <scene name='Sandbox_orly/C-terminal_helix/2'>C-ter</scene>. | Since prior experiments show that the last six residues are crucial for its dual targeting <ref> PMID 21440554 </ref>, a structural comparison has been performed looking at the <scene name='Sandbox_orly/C-terminal_helix/2'>C-ter</scene>. | ||
It was found that an important salt bridge exists in yeast aconitase where a <scene name='Sandbox_orly/Hydrophbic_pocket/3'>hydrophobic pocket</scene> exists instead in bovine aconitase ,in a very conserved area. This difference may be the underlying reason for the difference in the protein's behavior between different species. | It was found that an important salt bridge exists in yeast aconitase where a <scene name='Sandbox_orly/Hydrophbic_pocket/3'>hydrophobic pocket</scene> exists instead in bovine aconitase ,in a very conserved area. This difference may be the underlying reason for the difference in the protein's behavior between different species. | ||
Revision as of 11:57, 6 September 2012
Usage of bovine aconitase as a template for homology modelling of yeast aconitase
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- ↑ Regev-Rudzki N, Karniely S, Ben-Haim NN, Pines O. Yeast aconitase in two locations and two metabolic pathways: seeing small amounts is believing. Mol Biol Cell. 2005 Sep;16(9):4163-71. Epub 2005 Jun 22. PMID:15975908 doi:10.1091/mbc.E04-11-1028
- ↑ Zhang Y. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics. 2008 Jan 23;9:40. PMID:18215316 doi:10.1186/1471-2105-9-40
- ↑ Ben-Menachem R, Regev-Rudzki N, Pines O. The aconitase C-terminal domain is an independent dual targeting element. J Mol Biol. 2011 Jun 3;409(2):113-23. Epub 2011 Apr 6. PMID:21440554 doi:10.1016/j.jmb.2011.03.045
