5XGV

The structure of Diels-Alderase PyrE3 in the biosynthetic pathway of pyrroindomycins

Summary for 5XGV

• Entry DOI: 10.2210/pdb5xgv/pdb
• Descriptor: PyrE3, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: diels-alderase, pyrroindomycins, oxidoreductase
• Biological source: Streptomyces rugosporus
• Total number of polymer chains: 2
• Total formula weight: 100136.34

Authors

Pan, L.,Gong, Y.,Guo, Y. (deposition date: 2017-04-18, release date: 2018-04-25, Last modification date: 2023-11-22)

Primary citation

Zheng, Q.,Gong, Y.,Guo, Y.,Zhao, Z.,Wu, Z.,Zhou, Z.,Chen, D.,Pan, L.,Liu, W.
Structural Insights into a Flavin-Dependent [4 + 2] Cyclase that Catalyzes trans-Decalin Formation in Pyrroindomycin Biosynthesis.
Cell Chem Biol, 25:718-727.e3, 2018

PubMed Abstract: Here, we provide structural insights into PyrE3, a flavin-dependent [4 + 2] cyclase that catalyzes trans-decalin formation in the biosynthesis of pyrroindomycins. PyrE3 shares an architecture/domain organization head-to-tail similarity with the members of the family of para-hydroxybenzoate hydroxylase (pHBH)-fold monooxygenases, and possesses a flavin adenine dinucleotide (FAD)-binding domain, a middle domain, and a C-terminal thioredoxin-like domain. The FAD-binding domain forms a central hub of the protein structure, and binds with FAD in a "closed" conformation of pHBH-fold family monooxygenases known for their highly dynamic catalytic processes. FAD plays an essential structural role in PyrE3, where it is amenable to redox change; however, redox change has little effect on [4 + 2] cyclization activity. PyrE3 appears to selectively accommodate a tetramate-containing, linear polyene intermediate in a highly positively charged pocket, which is located at the interface between the FAD-binding domain and the middle domain, and can accelerate trans-decalin formation likely through an endo-selective [4 + 2] transition state.

PubMed: 29657086
DOI: 10.1016/j.chembiol.2018.03.007

Experimental method

X-RAY DIFFRACTION (2.099 Å)