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PreprintCited by 6Plant biochemistry and biosynthesisMicrobial Natural Products and BiosynthesisEnzyme Structure and Function

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Molecular insights into a distinct class of terpenoid cyclases

Open access
Guo, Rey-Ting, Li, Siyu, Huang, Jian-Wen, Min, Jian, Li, Hao, Ning, Meidan, Zhou, Shuyu, Yang, Yu, Chen, Chun-Chi·2024·Nature Communications
DOI 10.21203/rs.3.rs-4382230/v1PMC PMC11695735

Preprint — published as 10.1038/s41467-024-55717-6 · Paper page

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Abstract

Terpenoid cyclases (TCs) account for the synthesis of the most widespread and diverse natural compounds. A sesquiterpene cyclase termed BcABA3 from an abscisic acid-producing fungus Botrytis cinerea that yields (2 Z,4 E)-a-ionylideneethane but lacks signature feature of canonical TCs represents a distinct type of TCs. Here, we report the crystal structures of BcABA3, a closely related RuABA3 from Rutstroemia sp. and a bacterial SkABA3 from Shimazuella kribbensis. These ABA3 proteins adopt an all-a-helix fold and bind pyrophosphate moiety of farnesyl pyrophosphate by Glu-chelated Mg 2+ ion cluster. We conduct mutagenesis experiments to validate the role of the substrate-binding residues. SkABA3 appears to yield compounds that are distinct from (2 Z,4 E)-a-ionylideneethane. These results not only provide the molecular insight into ABA3 proteins that serve as an important basis to the future investigation of this class of TCs, but also reveal the existence of more uncharacterized terpenoids synthesized via dedicated machineries.

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Metadata

Authors
Guo, R.-T., Li, S., Huang, J.-W., Min, J., Li, H., Ning, M., Zhou, S., Yang, Y., & Chen, C.-C.
Affiliations
  • Hangzhou Normal University (CN)
  • State Key Laboratory of Biocatalysis and Enzyme Engineering (CN)
Corresponding author
  • Guo, Rey-Ting
  • Yang, Yu
  • Chen, Chun-Chi
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2024-12-23
Volume
16
Issue
1
Pages
207-207
ISSN
2041-1723 (ISSN-L)
DOI
10.21203/rs.3.rs-4382230/v1
PMC
PMC11695735
OpenAlex
W4406016718
Cited by
6
References
1
Citations by year
2026: 5 · 2025: 1
FWCI
1.79
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by-nc-nd)
  • Research Square (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • National Natural Science Foundation of China (32371307, 82341210, 32371307 and 82341210)
  • National Synchrotron Radiation Research Center
  • National Key Research and Development Program of China (2021YFC2104000)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant biochemistry and biosynthesis
  • Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Microbial Natural Products and Biosynthesis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords
sesquiterpene cyclase, Botrytis cinerea, substrate binding residues, abscisic acid biosynthesis, crystal structure, enzyme mechanism
MeSH terms
Abscisic Acid, Bacterial Proteins, Fungal Proteins, Isomerases, Magnesium, Models, Molecular, Polyisoprenyl Phosphates, Sesquiterpenes, Terpenes, Crystallography, X-Ray, Alkyl and Aryl Transferases, Botrytis

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