The structural and functional investigation into an unusual nitrile synthase

Hao Li, Jian-Wen Huang, Longhai Dai, Haibin Zheng, Si Dai, Qishan Zhang, Licheng Yao, Yunyun Yang, Yu Yang, Jian Min, Rey-Ting Guo () and Chun-Chi Chen ()
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Hao Li: Hubei University
Jian-Wen Huang: Hubei University
Longhai Dai: Hubei University
Haibin Zheng: Hubei University
Si Dai: Hubei University
Qishan Zhang: Hubei University
Licheng Yao: Hubei Gongtong Steroid Drug Research Institute
Yunyun Yang: Hubei University
Yu Yang: Hubei University
Jian Min: Hubei University
Rey-Ting Guo: Hubei University
Chun-Chi Chen: Hubei University

Nature Communications, 2023, vol. 14, issue 1, 1-9

Abstract: Abstract The biosynthesis of neurotoxin aetokthonotoxin (AETX) that features a unique structure of pentabrominated biindole nitrile involves a first-of-its-kind nitrile synthase termed AetD, an enzyme that shares very low sequence identity to known structures and catalyzes an unprecedented mechanism. In this study, we resolve the crystal structure of AetD in complex with the substrate 5,7-di-Br-L-Trp. AetD adopts the heme oxygenase like fold and forms a hydrophobic cavity within a helical bundle to accommodate the indole moiety. A diiron cluster comprising two irons that serves as a catalytic center binds to the carboxyl O and the amino N of the substrate. Notably, we demonstrate that the AetD-catalyzed reaction is independent of the bromination of the substrate and also solved crystal structures of AetD in complex with 5-Br-L-Trp and L-Trp. Altogether, the present study reveals the substrate-binding pattern and validates the diiron cluster-comprising active center of AetD, which should provide important basis to support the mechanistic investigations into this class of nitrile synthase.

Date: 2023
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DOI: 10.1038/s41467-023-43285-0

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