Structural highlights
Publication Abstract from 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.
Structure of homoserine O-acetyltransferase from Staphylococcus aureus: the first Gram-positive ortholog structure.,Thangavelu B, Pavlovsky AG, Viola R Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1340-5. doi:, 10.1107/S2053230X14018664. Epub 2014 Sep 25. PMID:25286936[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Thangavelu B, Pavlovsky AG, Viola R. Structure of homoserine O-acetyltransferase from Staphylococcus aureus: the first Gram-positive ortholog structure. Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1340-5. doi:, 10.1107/S2053230X14018664. Epub 2014 Sep 25. PMID:25286936 doi:http://dx.doi.org/10.1107/S2053230X14018664
