5Z53

Crystal structure of a cyclase Filc from Fischerella sp. in complex with cyclo-L-Arg-D-Pro

5Z53 の概要

• エントリーDOI: 10.2210/pdb5z53/pdb
• 分子名称: 12-epi-hapalindole U synthase, CALCIUM ION, amino({3-[(3S,8aS)-1,4-dioxooctahydropyrrolo[1,2-a]pyrazin-3-yl]propyl}amino)methaniminium, ... (5 entities in total)
• 機能のキーワード: prenyltransferase, transferase
• 由来する生物種: Fischerella sp. TAU
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 100257.12

構造登録者

Hu, X.Y.,Liu, W.D.,Chen, C.C.,Guo, R.T. (登録日: 2018-01-16, 公開日: 2018-12-19, 最終更新日: 2023-11-22)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.86 Å)