1w7m
From Proteopedia
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| - | [[Image:1w7m.gif|left|200px]]<br /> | + | [[Image:1w7m.gif|left|200px]]<br /><applet load="1w7m" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1w7m" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1w7m, resolution 2.70Å" /> | caption="1w7m, resolution 2.70Å" /> | ||
'''CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE I IN COMPLEX WITH L-PHE'''<br /> | '''CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE I IN COMPLEX WITH L-PHE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1W7M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with DPN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cysteine-S-conjugate_beta-lyase Cysteine-S-conjugate beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.13 4.4.1.13] | + | 1W7M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with DPN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cysteine-S-conjugate_beta-lyase Cysteine-S-conjugate beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.13 4.4.1.13] Known structural/functional Site: <scene name='pdbsite=AC2:Dpn Binding Site For Chain A'>AC2</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W7M OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:33:29 2007'' |
Revision as of 16:23, 18 December 2007
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CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE I IN COMPLEX WITH L-PHE
Overview
The kynurenine pathway has long been regarded as a valuable target for the, treatment of several neurological disorders accompanied by unbalanced, levels of metabolites along the catabolic cascade, kynurenic acid among, them. The irreversible transamination of kynurenine is the sole source of, kynurenic acid, and it is catalyzed by different isoforms of the, 5'-pyridoxal phosphate-dependent kynurenine aminotransferase (KAT). The, KAT-I isozyme has also been reported to possess beta-lyase activity toward, several sulfur- and selenium-conjugated molecules, leading to the proposal, of a role of the enzyme in carcinogenesis associated with environmental, pollutants. We solved the structure of human KAT-I in its 5'-pyridoxal, phosphate and pyridoxamine phosphate forms and in complex with the, competing substrate l-Phe. The enzyme active site revealed a striking, crown of aromatic residues decorating the ligand binding pocket, which we, propose as a major molecular determinant for substrate recognition., Ligand-induced conformational changes affecting Tyr(101) and the, Trp(18)-bearing alpha-helix H1 appear to play a central role in catalysis., Our data reveal a key structural role of Glu(27), providing a molecular, basis for the reported loss of enzymatic activity displayed by the, equivalent Glu --> Gly mutation in KAT-I of spontaneously hypertensive, rats.
About this Structure
1W7M is a Single protein structure of sequence from Homo sapiens with DPN as ligand. Active as Cysteine-S-conjugate beta-lyase, with EC number 4.4.1.13 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of human kynurenine aminotransferase I., Rossi F, Han Q, Li J, Li J, Rizzi M, J Biol Chem. 2004 Nov 26;279(48):50214-20. Epub 2004 Sep 10. PMID:15364907
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