6TTN

N-terminally truncated hyoscyamine 6-hydroxylase (tH6H) in complex with N-oxalylglycine and hyoscyamine

6TTN の概要

• エントリーDOI: 10.2210/pdb6ttn/pdb
• 関連するPDBエントリー: 6TTM 6TTO
• 分子名称: Hyoscyamine 6 beta-hydroxylase, N-OXALYLGLYCINE, 1,2-ETHANEDIOL, ... (9 entities in total)
• 機能のキーワード: jelly-roll, non-heme, 2-oxoglutarate, oxidoreductase
• 由来する生物種: Datura metel (Hindu datura)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37139.52

構造登録者

Kluza, A.,Mrugala, B.,Porebski, P.J.,Kurpiewska, K.,Niedzialkowska, E.,Weiss, M.S.,Borowski, T. (登録日: 2019-12-29, 公開日: 2020-03-18, 最終更新日: 2024-11-06)

主引用文献

Kluza, A.,Wojdyla, Z.,Mrugala, B.,Kurpiewska, K.,Porebski, P.J.,Niedzialkowska, E.,Minor, W.,Weiss, M.S.,Borowski, T.
Regioselectivity of hyoscyamine 6 beta-hydroxylase-catalysed hydroxylation as revealed by high-resolution structural information and QM/MM calculations.
Dalton Trans, 49:4454-4469, 2020

PubMed Abstract: Hyoscyamine 6β-hydroxylase (H6H) is a bifunctional non-heme 2-oxoglutarate/Fe2+-dependent dioxygenase that catalyzes the two final steps in the biosynthesis of scopolamine. Based on high resolution crystal structures of H6H from Datura metel, detailed information on substrate binding was obtained that provided insights into the onset of the enzymatic process. In particular, the role of two prominent residues was revealed - Glu-116 that interacts with the tertiary amine located on the hyoscyamine tropane moiety and Tyr-326 that forms CH-π hydrogen bonds with the hyoscyamine phenyl ring. The structures were used as the basis for QM/MM calculations that provided an explanation for the regioselectivity of the hydroxylation reaction on the hyoscyamine tropane moiety (C6 vs. C7) and quantified contributions of active site residues to respective barrier heights.

PubMed: 32182320
DOI: 10.1039/d0dt00302f

実験手法

X-RAY DIFFRACTION (1.12 Å)