6A9F

Crystal structure of a cyclase from Fischerella sp. TAU in complex with 4-(1H-Indol-3-yl)butan-2-one

Summary for 6A9F

• Entry DOI: 10.2210/pdb6a9f/pdb
• Descriptor: aromatic prenyltransferase, MAGNESIUM ION, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: prenyltransferase, transferase
• Biological source: Mastigocladus laminosus UTEX LB 1931
• Total number of polymer chains: 4
• Total formula weight: 97139.98

Authors

Hu, X.Y.,Liu, W.D.,Chen, C.C.,Guo, R.T. (deposition date: 2018-07-13, release date: 2018-12-19, Last modification date: 2023-11-22)

Primary citation

Chen, C.C.,Hu, X.,Tang, X.,Yang, Y.,Ko, T.P.,Gao, J.,Zheng, Y.,Huang, J.W.,Yu, Z.,Li, L.,Han, S.,Cai, N.,Zhang, Y.,Liu, W.,Guo, R.T.
The Crystal Structure of a Class of Cyclases that Catalyze the Cope Rearrangement
Angew. Chem. Int. Ed. Engl., 57:15060-15064, 2018

PubMed Abstract: Found recently in stignomatales, the Stig cyclases catalyze the Cope rearrangement and intramolecular cyclization to produce complex indole alkaloids. Five crystal structures were solved of subfamily 1 and 2 Stig cyclases, which adopt a β-sandwich fold like the non-catalytic carbohydrate-binding motif. Several complex structures were also determined of indole-based compounds, which are bound to the hydrophobic terminal cavity, where a conserved Asp residue makes an H-bond to the indole N and triggers the acid-catalyzed Cope rearrangement. Through analyzing the enzyme-ligand interactions and mutagenesis experiments, several aromatic residues were found important in catalysis. Apart from a common substrate binding mode and catalytic mechanism, potential subfamily variations that may attribute to the different product specificity are implicated. These results shall expand our scope of enzymology, in particular for further investigation of the biosynthetic Cope rearrangement.

PubMed: 30222239
DOI: 10.1002/anie.201808231

Experimental method

X-RAY DIFFRACTION (1.7 Å)