1ivr

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[[Image:1ivr.gif|left|200px]]
[[Image:1ivr.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1ivr |SIZE=350|CAPTION= <scene name='initialview01'>1ivr</scene>, resolution 2.4&Aring;
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The line below this paragraph, containing "STRUCTURE_1ivr", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CBA:N-PYRIDOXYL-2,3-DIHYDROXYASPARTIC+ACID-5-MONOPHOSPHATE'>CBA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1ivr| PDB=1ivr | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ivr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivr OCA], [http://www.ebi.ac.uk/pdbsum/1ivr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ivr RCSB]</span>
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}}
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'''STRUCTURE OF ASPARTATE AMINOTRANSFERASE'''
'''STRUCTURE OF ASPARTATE AMINOTRANSFERASE'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Stosch, A Graf Von.]]
[[Category: Stosch, A Graf Von.]]
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[[Category: aspartate aminotransferase]]
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[[Category: Aspartate aminotransferase]]
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[[Category: carbinolamine]]
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[[Category: Carbinolamine]]
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[[Category: erythro-beta-hydroxyaspartate]]
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[[Category: Erythro-beta-hydroxyaspartate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:28:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:25:18 2008''
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Revision as of 17:28, 2 May 2008

Template:STRUCTURE 1ivr

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

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