2b61 | pdb_00002b61

Crystal Structure of Homoserine Transacetylase

spinqualitylabelsall models 2b61, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2b61 is a 1 chain structure with sequence from "bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Gene: metX, met2 ("Bacterium influenzae" Lehmann and Neumann 1896) Activity: Homoserine O-acetyltransferase, with EC number 2.3.1.31 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [METX_HAEIN] Involved in the methionine biosynthesis. Catalyzes the transfer of the acetyl group from acetyl-CoA to the hydroxyl group of L-homoserine to yield O-acetyl-L-homoserine. 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 Homoserine transacetylase catalyzes one of the required steps in the biosynthesis of methionine in fungi and several bacteria. We have determined the crystal structure of homoserine transacetylase from Haemophilus influenzae to a resolution of 1.65 A. The structure identifies this enzyme to be a member of the alpha/beta-hydrolase structural superfamily. The active site of the enzyme is located near the end of a deep tunnel formed by the juxtaposition of two domains and incorporates a catalytic triad involving Ser143, His337, and Asp304. A structural basis is given for the observed double displacement kinetic mechanism of homoserine transacetylase. Furthermore, the properties of the tunnel provide a rationale for how homoserine transacetylase catalyzes a transferase reaction vs hydrolysis, despite extensive similarity in active site architecture to hydrolytic enzymes. Crystal structure of homoserine transacetylase from Haemophilus influenzae reveals a new family of alpha/beta-hydrolases.,Mirza IA, Nazi I, Korczynska M, Wright GD, Berghuis AM Biochemistry. 2005 Dec 6;44(48):15768-73. PMID:16313180 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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