This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Sandbox orly

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 6: Line 6:
Here it is possible to see the bovine aconitase that served as a template for the modeling. It is a large and stable protein with many secondary structures (here the <scene name='Sandbox_orly/Helices/1'> are emphesized </scene> as an example).
Here it is possible to see the bovine aconitase that served as a template for the modeling. It is a large and stable protein with many secondary structures (here the <scene name='Sandbox_orly/Helices/1'> are emphesized </scene> as an example).
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='Sandbox_orly/Hydrophbic_pocket/1'>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/1'>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.
</StructureSection>
</StructureSection>
<references/>
<references/>

Revision as of 11:36, 6 September 2012

Usage of bovine aconitase as a template for homology modelling of yeast aconitase

Structure bovine aconitase(PDB entry 1aco)

Drag the structure with the mouse to rotate
  1. 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
  2. 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
  3. 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
Personal tools