5TKA

Structure of the HD-domain phosphohydrolase OxsA

5TKA の概要

• エントリーDOI: 10.2210/pdb5tka/pdb
• 関連するPDBエントリー: 5TK6 5TK7 5TK8 5TK9
• 分子名称: OxsA protein, MAGNESIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: oxetanocin, hd-domain phosphohydrolase, metalloprotein, metal binding protein
• 由来する生物種: Bacillus megaterium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22796.22

構造登録者

Bridwell-Rabb, J.,Drennan, C.L. (登録日: 2016-10-06, 公開日: 2016-11-16, 最終更新日: 2023-10-04)

主引用文献

Bridwell-Rabb, J.,Kang, G.,Zhong, A.,Liu, H.W.,Drennan, C.L.
An HD domain phosphohydrolase active site tailored for oxetanocin-A biosynthesis.
Proc. Natl. Acad. Sci. U.S.A., 113:13750-13755, 2016

PubMed Abstract: HD domain phosphohydrolase enzymes are characterized by a conserved set of histidine and aspartate residues that coordinate an active site metallocenter. Despite the important roles these enzymes play in nucleotide metabolism and signal transduction, few have been both biochemically and structurally characterized. Here, we present X-ray crystal structures and biochemical characterization of the Bacillus megaterium HD domain phosphohydrolase OxsA, involved in the biosynthesis of the antitumor, antiviral, and antibacterial compound oxetanocin-A. These studies reveal a previously uncharacterized reaction for this family; OxsA catalyzes the conversion of a triphosphorylated compound into a nucleoside, releasing one molecule of inorganic phosphate at a time. Remarkably, this functionality is a result of the OxsA active site, which based on structural and kinetic analyses has been tailored to bind the small, four-membered ring of oxetanocin-A over larger substrates. Furthermore, our OxsA structures show an active site that switches from a dinuclear to a mononuclear metal center as phosphates are eliminated from substrate.

PubMed: 27849620
DOI: 10.1073/pnas.1613610113

実験手法

X-RAY DIFFRACTION (2.048 Å)