Title: Structure of homoserine O-acetyltransferase from Staphylococcus aureus: the first Gram-positive ortholog structure Thangavelu B, Pavlovsky AG, Viola R Ref: Acta Crystallographica F Struct Biol Commun, 70:1340, 2014 : PubMed
Homoserine O-acetyltransferase (HTA) catalyzes the formation of L-O-acetyl-homoserine from L-homoserine through the transfer of an acetyl group from acetyl-CoA. This is the first committed step required for the biosynthesis of methionine in many fungi, Gram-positive bacteria and some Gram-negative bacteria. The structure of HTA from Staphylococcus aureus (SaHTA) has been determined to a resolution of 2.45 A. The structure belongs to the alpha/beta-hydrolase superfamily, consisting of two distinct domains: a core alpha/beta-domain containing the catalytic site and a lid domain assembled into a helical bundle. The active site consists of a classical catalytic triad located at the end of a deep tunnel. Structure analysis revealed some important differences for SaHTA compared with the few known structures of HTA.
Representative scheme of Homoserine_transacetylase structure and an image from PDBsum server
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