5YNU

Crystal structure of an aromatic prenyltransferase FAMD1 from Fischerella ambigua UTEX 1903 in complex with INN

Summary for 5YNU

• Entry DOI: 10.2210/pdb5ynu/pdb
• Descriptor: aromatic prenyltransferase, 3-[(Z)-2-isocyanoethenyl]-1H-indole, IMIDAZOLE, ... (7 entities in total)
• Functional Keywords: prenyltransferase, transferase
• Biological source: Fischerella ambigua UTEX 1903
• Total number of polymer chains: 2
• Total formula weight: 75173.69

Authors

Wang, J.,Liu, W.D.,Chen, C.C.,Guo, R.T. (deposition date: 2017-10-25, release date: 2018-08-29, Last modification date: 2024-03-27)

Primary citation

Wang, J.,Chen, C.C.,Yang, Y.,Liu, W.,Ko, T.P.,Shang, N.,Hu, X.,Xie, Y.,Huang, J.W.,Zhang, Y.,Guo, R.T.
Structural insight into a novel indole prenyltransferase in hapalindole-type alkaloid biosynthesis.
Biochem. Biophys. Res. Commun., 495:1782-1788, 2018

PubMed 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.

PubMed: 29229390
DOI: 10.1016/j.bbrc.2017.12.039

Experimental method

X-RAY DIFFRACTION (1.7 Å)