4LD7

Crystal structure of AnaPT from Neosartorya fischeri

4LD7 の概要

• エントリーDOI: 10.2210/pdb4ld7/pdb
• 分子名称: Dimethylallyl tryptophan synthase, TRIHYDROGEN THIODIPHOSPHATE, SODIUM ION (3 entities in total)
• 機能のキーワード: abba-prenyltransferase, prenyltransferase, transferase
• 由来する生物種: Neosartorya fischeri
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 802327.68

構造登録者

Zocher, G.,Stehle, T. (登録日: 2013-06-24, 公開日: 2013-12-11, 最終更新日: 2024-02-28)

主引用文献

Yu, X.,Zocher, G.,Xie, X.,Liebhold, M.,Schutz, S.,Stehle, T.,Li, S.M.
Catalytic Mechanism of Stereospecific Formation of cis-Configured Prenylated Pyrroloindoline Diketopiperazines by Indole Prenyltransferases.
Chem.Biol., 20:1492-1501, 2013

PubMed Abstract: Indole prenyltransferases AnaPT, CdpC3PT, and CdpNPT are known to catalyze the formation of prenylated pyrroloindoline diketopiperazines from tryptophan-containing cyclic dipeptides in one-step reactions. In this study, we investigated the different stereoselectivities of these enzymes toward all the stereoisomers of cyclo-Trp-Ala and cyclo-Trp-Pro. The stereoselectivities of AnaPT and CdpC3PT mainly depend on the configuration of the tryptophanyl moiety in the substrates, and they usually introduce the prenyl moiety from the opposite sides. CdpNPT showed lower stereoselectivity, and the structure of the second amino acid moiety in the substrates is important for the stereospecificity in its enzyme catalysis. Moreover, we determined the crystal structure of AnaPT in complex with thiolodiphosphate and compared it with the known structures of CdpNPT. Our results clearly revealed the presence of an indole binding mode that has so far not been characterized.

PubMed: 24239009
DOI: 10.1016/j.chembiol.2013.10.007

実験手法

X-RAY DIFFRACTION (2.83 Å)