1yiy

Aedes aegypti kynurenine aminotransferase

spinqualitylabelsall models 1yiy, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1yiy is a 2 chain structure with sequence from Aedes aegypti. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: BR, PMP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KAT_AEDAE Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA) (PubMed:12110301, PubMed:15556614). Also catalyzes the irreversible transamination of several amino acids including cysteine, tyrosine, glutamine, methionine, histidine and phenylalanine (PubMed:15556614). Can use various keto-acids as the amino group acceptor (PubMed:15556614, PubMed:12110301). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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