5Y7C

Hapalindole A and DMSPP Bound AmbP3

5Y7C の概要

• エントリーDOI: 10.2210/pdb5y7c/pdb
• 分子名称: AmbP3, DIMETHYLALLYL S-THIOLODIPHOSPHATE, Hapalindole A, ... (4 entities in total)
• 機能のキーワード: prenyltransferase, transferase
• 由来する生物種: Fischerella ambigua UTEX 1903
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77290.29

構造登録者

Wong, C.P.,Awakawa, T.,Nakashima, Y. (登録日: 2017-08-16, 公開日: 2018-07-18, 最終更新日: 2023-11-22)

主引用文献

Wong, C.P.,Awakawa, T.,Nakashima, Y.,Mori, T.,Zhu, Q.,Liu, X.,Abe, I.
Two Distinct Substrate Binding Modes for the Normal and Reverse Prenylation of Hapalindoles by the Prenyltransferase AmbP3
Angew. Chem. Int. Ed. Engl., 57:560-563, 2018

PubMed Abstract: The cyanobacterial prenyltransferase AmbP3 catalyzes the reverse prenylation of the tetracyclic indole alkaloid hapalindole U at its C-2 position. Interestingly, AmbP3 also accepts hapalindole A, a halogenated C-10 epimer of hapalindole U, and catalyzes normal prenylation at its C-2 position. The comparison of the two ternary crystal structures, AmbP3-DMSPP/hapalindole U and AmbP3-DMSPP/hapalindole A, at 1.65-2.00 Å resolution revealed two distinct orientations for the substrate binding that define reverse or normal prenylation. The tolerance of the enzyme for these altered orientations is attributed to the hydrophobicity of the substrate binding pocket and the plasticity of the amino acids surrounding the allyl group of the prenyl donor. This is the first study to provide the intimate structural basis for the normal and reverse prenylations catalyzed by a single enzyme, and it offers novel insight into the engineered biosynthesis of prenylated natural products.

PubMed: 29178634
DOI: 10.1002/anie.201710682

実験手法

X-RAY DIFFRACTION (2.003 Å)