1ivr
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1ivr.gif|left|200px]] | [[Image:1ivr.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1ivr", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1ivr| PDB=1ivr | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''STRUCTURE OF ASPARTATE AMINOTRANSFERASE''' | '''STRUCTURE OF ASPARTATE AMINOTRANSFERASE''' | ||
| Line 27: | Line 24: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Stosch, A Graf Von.]] | [[Category: Stosch, A Graf Von.]] | ||
| - | [[Category: | + | [[Category: Aspartate aminotransferase]] |
| - | [[Category: | + | [[Category: Carbinolamine]] |
| - | [[Category: | + | [[Category: Erythro-beta-hydroxyaspartate]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:28:41 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:28, 2 May 2008
STRUCTURE OF ASPARTATE AMINOTRANSFERASE
Overview
The crystal structure of mitochondrial aspartate aminotransferase (mAAT) of chicken complexed with erythro-beta-hydroxyaspartate has been determined at 2.4 A resolution. Pregrown crystals of mAAT complexed with the inhibitor maleate (closed enzyme conformation, orthorhombic space group C222(1)) were soaked in solutions of erythro-beta-hydroxyaspartate. The ligand exchange was monitored by microspectrophotometry. The active site turned out to be predominantly occupied by the carbinolamine intermediate. The carbinolamine is a true intermediate of the catalytic cycle forming the last covalently bound enzyme:substrate complex before release of the keto acid product. Occupancies of approximately 80% for the carbinolamine and of approximately 20% for the quinonoid intermediate were obtained. Two hydrogen bonds were identified that are potentially relevant for the accumulation of the carbinolamine intermediate: one to the hydroxyl group of Tyr 70* and the other to the epsilon-NH2 group of Lys 258.
About this Structure
1IVR is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Aspartate aminotransferase complexed with erythro-beta-hydroxyaspartate: crystallographic and spectroscopic identification of the carbinolamine intermediate., von Stosch AG, Biochemistry. 1996 Dec 3;35(48):15260-8. PMID:8952476 Page seeded by OCA on Fri May 2 20:28:41 2008
