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Structure of homoserine O ‐acetyltransferase from Staphylococcus aureus : the first Gram‐positive ortholog structure
Author(s) -
Thangavelu Bharani,
Pavlovsky Alexander G.,
Viola Ronald
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14018664
Subject(s) - bacteria , homoserine , acetyltransferase , catalytic triad , chemistry , staphylococcus aureus , microbiology and biotechnology , stereochemistry , active site , biology , enzyme , quorum sensing , biochemistry , gene , acetylation , genetics , biofilm
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 ( Sa HTA) has been determined to a resolution of 2.45 Å. The structure belongs to the α/β‐hydrolase superfamily, consisting of two distinct domains: a core α/β‐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 Sa HTA compared with the few known structures of HTA.