Crystal structure of an aromatic prenyltransferase in complex with ligand2Crystal structure of an aromatic prenyltransferase in complex with ligand2

Structural highlights

5ynv is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. 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

5ynv, resolution 1.70Å

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