1ivr
From Proteopedia
(New page: 200px<br /><applet load="1ivr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ivr, resolution 2.4Å" /> '''STRUCTURE OF ASPARTAT...) |
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| - | [[Image:1ivr.gif|left|200px]]<br /><applet load="1ivr" size=" | + | [[Image:1ivr.gif|left|200px]]<br /><applet load="1ivr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ivr, resolution 2.4Å" /> | caption="1ivr, resolution 2.4Å" /> | ||
'''STRUCTURE OF ASPARTATE AMINOTRANSFERASE'''<br /> | '''STRUCTURE OF ASPARTATE AMINOTRANSFERASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of mitochondrial aspartate aminotransferase (mAAT) | + | 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== | ==About this Structure== | ||
| - | 1IVR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CBA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1IVR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CBA:'>CBA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Stosch, A | + | [[Category: Stosch, A Graf Von.]] |
[[Category: CBA]] | [[Category: CBA]] | ||
[[Category: aspartate aminotransferase]] | [[Category: aspartate aminotransferase]] | ||
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[[Category: erythro-beta-hydroxyaspartate]] | [[Category: erythro-beta-hydroxyaspartate]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:16:11 2008'' |
Revision as of 11:16, 21 February 2008
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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 with as ligand. Active as Aspartate transaminase, with EC number 2.6.1.1 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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