7F14

Crystal structure of isomerase Dcr3 complex with substrate analogue 3

7F14 の概要

• エントリーDOI: 10.2210/pdb7f14/pdb
• 分子名称: Dcr3, methyl 2-[2,6-bis(oxidanyl)phenyl]carbonyl-5-methyl-3-oxidanyl-benzoate (3 entities in total)
• 機能のキーワード: tetrahydroxanthones, blennolides, isomerase
• 由来する生物種: Diaporthe longicolla
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39844.64

構造登録者

Yang, J.,Mori, T.,Abe, I. (登録日: 2021-06-07, 公開日: 2022-04-20, 最終更新日: 2023-11-29)

主引用文献

Yang, J.,Mori, T.,Wei, X.,Matsuda, Y.,Abe, I.
Structural Basis for Isomerization Reactions in Fungal Tetrahydroxanthone Biosynthesis and Diversification.
Angew.Chem.Int.Ed.Engl., 60:19458-19465, 2021

PubMed Abstract: The novel isomerase NsrQ, from Aspergillus novofumigatus, is a key enzyme in the biosynthesis of fungal tetrahydroxanthones and is responsible for dearomatizing cyclization to provide a tetrahydroxanthone scaffold. NsrQ catalyzes a two-step isomerization reaction, involving the isomerization of allylic alcohol and subsequent inversion of configuration at the methyl group. We report on the biochemical and structural characterizations of NsrQ, and its homologue Dcr3, from Diaporthe longicolla. The crystal structures of NsrQ and Dcr3 revealed their similar overall structures, with a cone-shaped α+β barrel fold, to those of the nuclear transport factor 2-like superfamily enzymes. Furthermore, the structures of Dcr3 and NsrQ variants complexed with substrate analogues and the site-directed mutagenesis studies identified the catalytic residues and the important hydrophobic residues in shaping the active site pocket for substrate binding. These enzymes thus utilize Glu and His residues as acid-base catalysts. Based on these observations, we proposed a detailed reaction mechanism for NsrQ-catalyzed isomerization reactions.

PubMed: 34180120
DOI: 10.1002/anie.202107884

実験手法

X-RAY DIFFRACTION (2.4 Å)