4QLO

Crystal Structure of homoserine o-acetyltransferase from Staphylococcus aureus

4QLO の概要

• エントリーDOI: 10.2210/pdb4qlo/pdb
• 分子名称: homoserine O-acetyltransferase (2 entities in total)
• 機能のキーワード: rossmann fold, acetyltransferase, acetylco-a binding, transferase
• 由来する生物種: Staphylococcus aureus subsp. aureus
• 細胞内の位置: Cytoplasm (By similarity): A8YYT5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41244.43

構造登録者

Thangavelu, B.,Pavlovsky, A.G.,Viola, R.E. (登録日: 2014-06-12, 公開日: 2014-08-20, 最終更新日: 2024-02-28)

主引用文献

Thangavelu, B.,Pavlovsky, A.G.,Viola, R.
Structure of homoserine O-acetyltransferase from Staphylococcus aureus: the first Gram-positive ortholog structure.
Acta Crystallogr.,Sect.F, 70:1340-1345, 2014

PubMed 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 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 SaHTA compared with the few known structures of HTA.

PubMed: 25286936
DOI: 10.1107/S2053230X14018664

実験手法

X-RAY DIFFRACTION (2.45 Å)