2b61
From Proteopedia
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Crystal Structure of Homoserine Transacetylase
Overview
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.
About this Structure
2B61 is a Single protein structure of sequence from Haemophilus influenzae. Active as Homoserine O-acetyltransferase, with EC number 2.3.1.31 Full crystallographic information is available from OCA.
Reference
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
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