Structural rearrangements of a polyketide synthase module during its catalytic cycle

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 () and Georgios Skiniotis ()
Additional contact information
Jonathan R. Whicher: Life Sciences Institute, University of Michigan
Somnath Dutta: Life Sciences Institute, University of Michigan
Douglas A. Hansen: Life Sciences Institute, 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
Janet L. Smith: Life Sciences Institute, University of Michigan
Georgios Skiniotis: Life Sciences Institute, University of Michigan

Nature, 2014, vol. 510, issue 7506, 560-564

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.

Date: 2014
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DOI: 10.1038/nature13409

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