Evidence map›Paper›PMID 33558520›Full record

ArticleNature communications2021

Structural basis for the biosynthesis of lovastatin.

Jialiang Wang, Jingdan Liang, Lu Chen, Wei Zhang, Liangliang Kong, Chao Peng, Chen Su, Yi Tang, Zixin Deng, Zhijun Wang

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
10.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed, 86 citations in OpenAlex.

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  6. The Diels-Alder Reaction as a Key Step in Natural Product Synthesis.Progress in the chemistry of organic natural products · 2026
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  15. Review
  16. The structure of full-length AFPK supports the ACP linker in a role that regulates iterative polyketide and fatty acid assembly.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Review
  19. Metabolomic insights intoFood science & nutrition · 2024
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 2 countries.

Jialiang Wang *State Key Laboratory of Microbial Metabolism and School of Life Science & Biotechnology, Shanghai Jiao Tong University, Shanghai, China.ORCID 0000-0003-1050-2912
Jingdan Liang *State Key Laboratory of Microbial Metabolism and School of Life Science & Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Lu ChenState Key Laboratory of Microbial Metabolism and School of Life Science & Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Wei ZhangState Key Laboratory of Microbial Metabolism and School of Life Science & Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
Liangliang KongNational Facility for Protein Science in Shanghai, Shanghai, China.
Chao PengNational Facility for Protein Science in Shanghai, Shanghai, China.ORCID 0000-0002-6814-2676
Chen SuNational Facility for Protein Science in Shanghai, Shanghai, China.
Yi TangDepartment of Chemical and Biomolecular Engineering and Department of Chemistry and Biochemistry, University of California, Los Angeles, CA, USA.
Zixin DengState Key Laboratory of Microbial Metabolism and School of Life Science & Biotechnology, Shanghai Jiao Tong University, Shanghai, China. zxdeng@sjtu.edu.cn.ORCID 0000-0003-0724-3390
Zhijun WangState Key Laboratory of Microbial Metabolism and School of Life Science & Biotechnology, Shanghai Jiao Tong University, Shanghai, China. wangzhijun@sjtu.edu.cn.ORCID 0000-0002-9221-2224
Shanghai Jiao Tong University · CNUniversity of California, Los Angeles · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Statins are effective cholesterol-lowering drugs. Lovastatin, one of the precursors of statins, is formed from dihydromonacolin L (DML), which is synthesized by lovastatin nonaketide synthase (LovB), with the assistance of a separate trans-acting enoyl reductase (LovC). A full DML synthesis comprises 8 polyketide synthetic cycles with about 35 steps. The assembling of the LovB-LovC complex, and the structural basis for the iterative and yet permutative functions of the megasynthase have remained a mystery. Here, we present the cryo-EM structures of the LovB-LovC complex at 3.60 Å and the core LovB at 2.91 Å resolution. The domain organization of LovB is an X-shaped face-to-face dimer containing eight connected domains. The binding of LovC laterally to the malonyl-acetyl transferase domain allows the completion of a L-shaped catalytic chamber consisting of six active domains. This architecture and the structural details of the megasynthase provide the basis for the processing of the intermediates by the individual catalytic domains. The detailed architectural model provides structural insights that may enable the re-engineering of the megasynthase for the generation of new statins.

Indexed as

BiocatalysisLovastatinModels, MolecularNaphthalenesOxidoreductases Acting on CH-CH Group DonorsPolyketide SynthasesProtein DomainsSubstrate Specificitydihydromonacolin LLovastatinNaphthalenesOxidoreductases Acting on CH-CH Group DonorsPolyketide Synthases

Identifiers

PMID33558520
PMCPMC7870829
OpenAlexW3127183542

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.