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Structure of homoserine O-acetyltransferase from Staphylococcus aureus: the first Gram-positive ortholog structure.


ABSTRACT: 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?Å. The structure belongs to the ?/?-hydrolase superfamily, consisting of two distinct domains: a core ?/?-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.

SUBMITTER: Thangavelu B 

PROVIDER: S-EPMC4188076 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature

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Structure of homoserine O-acetyltransferase from Staphylococcus aureus: the first Gram-positive ortholog structure.

Thangavelu Bharani B   Pavlovsky Alexander G AG   Viola Ronald R  

Acta crystallographica. Section F, Structural biology communications 20140925 Pt 10


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 Å. The structure belongs to the α/β-hydrolase superfamily, consisting of two distinct domai  ...[more]

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