5YK9

Crystal structure of selenomethionine-labelled indole prenyltransferase AmbP1

5YK9 の概要

• エントリーDOI: 10.2210/pdb5yk9/pdb
• 分子名称: AmbP1 (1 entity in total)
• 機能のキーワード: cyanobacteria, 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: 70684.52

構造登録者

Awakawa, T.,Nakashima, Y.,Liu, X.,Abe, I. (登録日: 2017-10-12, 公開日: 2018-06-06, 最終更新日: 2024-10-23)

主引用文献

Awakawa, T.,Mori, T.,Nakashima, Y.,Zhai, R.,Wong, C.P.,Hillwig, M.L.,Liu, X.,Abe, I.
Molecular Insight into the Mg2+-Dependent Allosteric Control of Indole Prenylation by Aromatic Prenyltransferase AmbP1
Angew. Chem. Int. Ed. Engl., 57:6810-6813, 2018

PubMed Abstract: AmbP1 is a cyanobacterial aromatic prenyltransferase and a dedicated synthase for (R)-3-geranyl-3-isocyanovinyl indolenine (2), the biogenetic precursor for hapalindole-type alkaloids. The regioselective geranylation of cis-indolyl vinyl isonitrile (1) by the standalone AmbP1 to give 2 has been shown to require a magnesium ion (Mg ) to suppress the formation of cis-2-geranylindolyl vinyl isonitrile (3). Here, we report high-resolution crystal structures of AmbP1 in complex with 1 and geranyl S-thiodiphosphate (GSPP) in the presence and absence of a Mg effector. The comparative study of these structures revealed a unique allosteric binding site for Mg that modulates the conformation of 1 in the active site of AmbP1 for its selective geranylation. This work defines the structural basis for AmbP1 catalysis in the biogenesis of hapalindole-type alkaloids and provides the first atomic-level insight to the allosteric regulation of prenyltransferases.

PubMed: 29677386
DOI: 10.1002/anie.201800855

実験手法

X-RAY DIFFRACTION (3.001 Å)