1ivr
From Proteopedia
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| - | [[Image:1ivr.gif|left|200px]] | + | [[Image:1ivr.gif|left|200px]] |
| - | + | ||
| - | '''STRUCTURE OF ASPARTATE AMINOTRANSFERASE''' | + | {{Structure |
| + | |PDB= 1ivr |SIZE=350|CAPTION= <scene name='initialview01'>1ivr</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CBA:N-PYRIDOXYL-2,3-DIHYDROXYASPARTIC ACID-5-MONOPHOSPHATE'>CBA</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF ASPARTATE AMINOTRANSFERASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IVR is a [ | + | 1IVR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8952476 8952476] |
[[Category: Aspartate transaminase]] | [[Category: Aspartate transaminase]] | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
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[[Category: erythro-beta-hydroxyaspartate]] | [[Category: erythro-beta-hydroxyaspartate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:55:32 2008'' |
Revision as of 09:55, 20 March 2008
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| , resolution 2.4Å | |||||||
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| Ligands: | |||||||
| Activity: | Aspartate transaminase, with EC number 2.6.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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