1yiy
From Proteopedia
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|PDB= 1yiy |SIZE=350|CAPTION= <scene name='initialview01'>1yiy</scene>, resolution 1.9Å | |PDB= 1yiy |SIZE=350|CAPTION= <scene name='initialview01'>1yiy</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene> | + | |LIGAND= <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=PMP:4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE'>PMP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= KAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7159 Aedes aegypti]) | |GENE= KAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7159 Aedes aegypti]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1yiz|1YIZ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yiy OCA], [http://www.ebi.ac.uk/pdbsum/1yiy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yiy RCSB]</span> | ||
}} | }} | ||
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[[Category: Robinson, H.]] | [[Category: Robinson, H.]] | ||
[[Category: Wilson, S.]] | [[Category: Wilson, S.]] | ||
| - | [[Category: BR]] | ||
| - | [[Category: PMP]] | ||
[[Category: aede]] | [[Category: aede]] | ||
[[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 01:09:02 2008'' |
Revision as of 22:09, 30 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | KAT (Aedes aegypti) | ||||||
| Related: | 1YIZ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Aedes aegypti kynurenine aminotransferase
Overview
Aedes aegypti kynurenine aminotransferase (AeKAT) catalyzes the irreversible transamination of kynurenine to kynurenic acid, the natural antagonist of NMDA and 7-nicotinic acetycholine receptors. Here, we report the crystal structure of AeKAT in its PMP and PLP forms at 1.90 and 1.55 A, respectively. The structure was solved by a combination of single-wavelength anomalous dispersion and molecular replacement approaches. The initial search model in the molecular replacement method was built with the result of single-wavelength anomalous dispersion data from the Br-AeKAT crystal in combination with homology modeling. The solved structure shows that the enzyme is a homodimer, and that the two subunits are stabilized by a number of hydrogen bonds, salts bridges, and hydrophobic interactions. Each subunit is divided into an N-terminal arm and small and large domains. Based on its folding, the enzyme belongs to the prototypical fold type, aminotransferase subgroup I. The three-dimensional structure shows a strictly conserved 'PLP-phosphate binding cup' featuring PLP-dependent enzymes. The interaction between Cys284 (A) and Cys284 (B) is unique in AeKAT, which might explain the cysteine effect of AeKAT activity. Further mutation experiments of this residue are needed to eventually understand the mechanism of the enzyme modulation by cysteine.
About this Structure
1YIY is a Single protein structure of sequence from Aedes aegypti. Full crystallographic information is available from OCA.
Reference
Crystal structures of Aedes aegypti kynurenine aminotransferase., Han Q, Gao YG, Robinson H, Ding H, Wilson S, Li J, FEBS J. 2005 May;272(9):2198-206. PMID:15853804
Page seeded by OCA on Mon Mar 31 01:09:02 2008
Categories: Aedes aegypti | Single protein | Ding, H. | Gao, Y G. | Han, Q. | Li, J. | Robinson, H. | Wilson, S. | Aede | Kynurenic acid | Kynurenine | Kynurenine aminotrasferase | Mosquito | Plp-enzyme | Pmp | Pyridoxamine phosphate | Transferase
