4YZJ

Crystal structure of selnomethionin-labeled indole prenyltransferase TleC

4YZJ の概要

• エントリーDOI: 10.2210/pdb4yzj/pdb
• 関連するPDBエントリー: 4YZK 4YZL
• 分子名称: Tryptophan dimethylallyltransferase (2 entities in total)
• 機能のキーワード: transferase, indole prenyltransferase, pt-fold, indolactam v, teleocidins
• 由来する生物種: Streptomyces blastmyceticus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43653.16

構造登録者

Mori, T.,Matsui, T.,Morita, H.,Abe, I. (登録日: 2015-03-25, 公開日: 2016-03-16, 最終更新日: 2024-11-06)

主引用文献

Mori, T.,Zhang, L.,Awakawa, T.,Hoshino, S.,Okada, M.,Morita, H.,Abe, I.
Manipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases.
Nat Commun, 7:10849-10849, 2016

PubMed Abstract: Prenylation reactions play crucial roles in controlling the activities of biomolecules. Bacterial prenyltransferases, TleC from Streptomyces blastmyceticus and MpnD from Marinactinospora thermotolerans, catalyse the 'reverse' prenylation of (-)-indolactam V at the C-7 position of the indole ring with geranyl pyrophosphate or dimethylallyl pyrophosphate, to produce lyngbyatoxin or pendolmycin, respectively. Using in vitro analyses, here we show that both TleC and MpnD exhibit relaxed substrate specificities and accept various chain lengths (C5-C25) of the prenyl donors. Comparisons of the crystal structures and their ternary complexes with (-)-indolactam V and dimethylallyl S-thiophosphate revealed the intimate structural details of the enzyme-catalysed 'reverse' prenylation reactions and identified the active-site residues governing the selection of the substrates. Furthermore, structure-based enzyme engineering successfully altered the preference for the prenyl chain length of the substrates, as well as the regio- and stereo-selectivities of the prenylation reactions, to produce a series of unnatural novel indolactams.

PubMed: 26952246
DOI: 10.1038/ncomms10849

実験手法

X-RAY DIFFRACTION (2.106 Å)