Structural highlights
Publication Abstract from PubMed
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 beta-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.
Structural insight into a novel indole prenyltransferase in hapalindole-type alkaloid biosynthesis.,Wang J, Chen CC, Yang Y, Liu W, Ko TP, Shang N, Hu X, Xie Y, Huang JW, Zhang Y, Guo RT Biochem Biophys Res Commun. 2018 Jan 8;495(2):1782-1788. doi:, 10.1016/j.bbrc.2017.12.039. Epub 2017 Dec 8. PMID:29229390[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang J, Chen CC, Yang Y, Liu W, Ko TP, Shang N, Hu X, Xie Y, Huang JW, Zhang Y, Guo RT. Structural insight into a novel indole prenyltransferase in hapalindole-type alkaloid biosynthesis. Biochem Biophys Res Commun. 2018 Jan 8;495(2):1782-1788. doi:, 10.1016/j.bbrc.2017.12.039. Epub 2017 Dec 8. PMID:29229390 doi:http://dx.doi.org/10.1016/j.bbrc.2017.12.039
