5ynw

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

Structural highlights 5ynw is a 2 chain structure with sequence from Fischerella utex1903. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , , Related: 5ynt, 5ynv, 5ynu Gene: ambP3 (Fischerella UTEX1903) 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 5ynw, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image