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Structural rearrangements of a polyketide synthase module during its catalytic cycle

Author

Listed:
  • Jonathan R. Whicher

    (Life Sciences Institute, University of Michigan
    Chemical Biology Graduate Program, University of Michigan)

  • Somnath Dutta

    (Life Sciences Institute, University of Michigan)

  • Douglas A. Hansen

    (Life Sciences Institute, University of Michigan
    University of Michigan)

  • Wendi A. Hale

    (University of Michigan)

  • Joseph A. Chemler

    (Life Sciences Institute, University of Michigan)

  • Annie M. Dosey

    (Life Sciences Institute, University of Michigan)

  • Alison R. H. Narayan

    (Life Sciences Institute, University of Michigan)

  • Kristina Håkansson

    (University of Michigan)

  • David H. Sherman

    (Life Sciences Institute, University of Michigan
    University of Michigan
    University of Michigan
    University of Michigan)

  • Janet L. Smith

    (Life Sciences Institute, University of Michigan
    University of Michigan)

  • Georgios Skiniotis

    (Life Sciences Institute, University of Michigan
    University of Michigan)

Abstract

Polyketide synthases (PKSs) are multidomain enzymes that produce polyketides, which form the basis of many therapeutic agents; here, electron cryo-microscopy is used to probe the structure of an intact module of a multi-enzyme PKS in different functional states.

Suggested Citation

  • Jonathan R. Whicher & Somnath Dutta & Douglas A. Hansen & Wendi A. Hale & Joseph A. Chemler & Annie M. Dosey & Alison R. H. Narayan & Kristina Håkansson & David H. Sherman & Janet L. Smith & Georgios , 2014. "Structural rearrangements of a polyketide synthase module during its catalytic cycle," Nature, Nature, vol. 510(7506), pages 560-564, June.
    • Handle: RePEc:nat:nature:v:510:y:2014:i:7506:d:10.1038_nature13409
    DOI: 10.1038/nature13409
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    Cited by:

    1. Thomas J. Booth & Kenan A. J. Bozhüyük & Jonathon D. Liston & Sibyl F. D. Batey & Ernest Lacey & Barrie Wilkinson, 2022. "Bifurcation drives the evolution of assembly-line biosynthesis," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Guifa Zhai & Yan Zhu & Guo Sun & Fan Zhou & Yangning Sun & Zhou Hong & Chuan Dong & Peter F. Leadlay & Kui Hong & Zixin Deng & Fuling Zhou & Yuhui Sun, 2023. "Insights into azalomycin F assembly-line contribute to evolution-guided polyketide synthase engineering and identification of intermodular recognition," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Jialiang Wang & Xiaojie Wang & Xixi Li & LiangLiang Kong & Zeqian Du & Dandan Li & Lixia Gou & Hao Wu & Wei Cao & Xiaozheng Wang & Shuangjun Lin & Ting Shi & Zixin Deng & Zhijun Wang & Jingdan Liang, 2023. "C–N bond formation by a polyketide synthase," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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