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Structural insight into a novel indole prenyltransferase in hapalindole-type alkaloid biosynthesis.

Abstract：

:FamD1 is a novel CloQ/NphB-family indole prenyltransferase which involves in hapalindole-type alkaloid biosynthesis. Here the native FamD1 structure and three protein-ligand complexes are analyzed to investigate the molecular basis of substrate binding and catalysis. FamD1 adopts a typical ABBA architecture of aromatic prenyltransferase, in which the substrate-binding chamber is found in the central β-barrel. The indole-containing acceptor substrate is bound adjacent to the prenyl donor. Based on the complex structures, a catalytic mechanism of FamD1 is proposed. Functional implications on the sister enzyme FamD2 are also discussed.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Wang J,Chen CC,Yang Y,Liu W,Ko TP,Shang N,Hu X,Xie Y,Huang JW,Zhang Y,Guo RT

doi

10.1016/j.bbrc.2017.12.039

subject

Has Abstract

pub_date

2018-01-08 00:00:00

pages

1782-1788

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(17)32431-2

journal_volume

495

pub_type

杂志文章

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