1w7m
From Proteopedia
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|PDB= 1w7m |SIZE=350|CAPTION= <scene name='initialview01'>1w7m</scene>, resolution 2.70Å | |PDB= 1w7m |SIZE=350|CAPTION= <scene name='initialview01'>1w7m</scene>, resolution 2.70Å | ||
|SITE= <scene name='pdbsite=AC2:Dpn+Binding+Site+For+Chain+A'>AC2</scene> | |SITE= <scene name='pdbsite=AC2:Dpn+Binding+Site+For+Chain+A'>AC2</scene> | ||
| - | |LIGAND= <scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene> | + | |LIGAND= <scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene>, <scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7m OCA], [http://www.ebi.ac.uk/pdbsum/1w7m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w7m RCSB]</span> | ||
}} | }} | ||
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[[Category: Rizzi, M.]] | [[Category: Rizzi, M.]] | ||
[[Category: Rossi, F.]] | [[Category: Rossi, F.]] | ||
| - | [[Category: DPN]] | ||
[[Category: aminotransferase]] | [[Category: aminotransferase]] | ||
[[Category: kynurenic acid]] | [[Category: kynurenic acid]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:32:21 2008'' |
Revision as of 21:32, 30 March 2008
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| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Cysteine-S-conjugate beta-lyase, with EC number 4.4.1.13 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Mon Mar 31 00:32:21 2008
