5ZM2

Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AndA

5ZM2 の概要

• エントリーDOI: 10.2210/pdb5zm2/pdb
• 分子名称: Dioxygenase andA (2 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Emericella variicolor (Aspergillus variecolor,Aspergillus stellatus)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 135417.61

構造登録者

Nakashima, Y.,Senda, T. (登録日: 2018-04-01, 公開日: 2018-07-18, 最終更新日: 2023-11-22)

主引用文献

Nakashima, Y.,Mitsuhashi, T.,Matsuda, Y.,Senda, M.,Sato, H.,Yamazaki, M.,Uchiyama, M.,Senda, T.,Abe, I.
Structural and Computational Bases for Dramatic Skeletal Rearrangement in Anditomin Biosynthesis.
J. Am. Chem. Soc., 140:9743-9750, 2018

PubMed Abstract: AndA, an Fe(II)/α-ketoglutarate (αKG)-dependent enzyme, is the key enzyme that constructs the unique and congested bridged-ring system of anditomin (1), by catalyzing consecutive dehydrogenation and isomerization reactions. Although we previously characterized AndA to some extent, the means by which the enzyme facilitates this drastic structural reconstruction have remained elusive. In this study, we have solved three X-ray crystal structures of AndA, in its apo form and in the complexes with Fe(II), αKG, and two substrates. The crystal structures and mutational experiments identified several key amino acid residues important for the catalysis and provided insight into how AndA controls the reaction. Furthermore, computational calculations validated the proposed reaction mechanism for the bridged-ring formation and also revealed the requirement of a series of conformational changes during the transformation.

PubMed: 29972643
DOI: 10.1021/jacs.8b06084

実験手法

X-RAY DIFFRACTION (2.5 Å)