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TitleStructural rearrangements of a polyketide synthase module during its catalytic cycle.
Journal, issue, pagesNature, Vol. 510, Issue 7506, Page 560-564, Year 2014
Publish dateJun 26, 2014
AuthorsJonathan 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 Skiniotis /
PubMed AbstractThe polyketide synthase (PKS) mega-enzyme assembly line uses a modular architecture to synthesize diverse and bioactive natural products that often constitute the core structures or complete chemical ...The polyketide synthase (PKS) mega-enzyme assembly line uses a modular architecture to synthesize diverse and bioactive natural products that often constitute the core structures or complete chemical entities for many clinically approved therapeutic agents. The architecture of a full-length PKS module from the pikromycin pathway of Streptomyces venezuelae creates a reaction chamber for the intramodule acyl carrier protein (ACP) domain that carries building blocks and intermediates between acyltransferase, ketosynthase and ketoreductase active sites (see accompanying paper). Here we determine electron cryo-microscopy structures of a full-length pikromycin PKS module in three key biochemical states of its catalytic cycle. Each biochemical state was confirmed by bottom-up liquid chromatography/Fourier transform ion cyclotron resonance mass spectrometry. The ACP domain is differentially and precisely positioned after polyketide chain substrate loading on the active site of the ketosynthase, after extension to the β-keto intermediate, and after β-hydroxy product generation. The structures reveal the ACP dynamics for sequential interactions with catalytic domains within the reaction chamber, and for transferring the elongated and processed polyketide substrate to the next module in the PKS pathway. During the enzymatic cycle the ketoreductase domain undergoes dramatic conformational rearrangements that enable optimal positioning for reductive processing of the ACP-bound polyketide chain elongation intermediate. These findings have crucial implications for the design of functional PKS modules, and for the engineering of pathways to generate pharmacologically relevant molecules.
External linksNature / PubMed:24965656 / PubMed Central
MethodsEM (single particle)
Resolution7.8 - 11.6 Å
Structure data

EMDB-5663:
Cryo-EM structure of Pentaketide-KS5-PikAIII
Method: EM (single particle) / Resolution: 7.9 Å

EMDB-5664:
Cryo-EM structure of beta-ketohexaketide-PikAIII
Method: EM (single particle) / Resolution: 7.8 Å

EMDB-5665:
Cryo-EM structure of beta-hydroxyhexaketide-PikAIII conformation 1
Method: EM (single particle) / Resolution: 10.7 Å

EMDB-5666:
Cryo-EM structure of beta-hydroxyhexaketide-PikAIII conformation 2
Method: EM (single particle) / Resolution: 11.0 Å

EMDB-5667:
Cryo-EM structure of beta-hydroxyhexaketide-PikAIII conformation 3
Method: EM (single particle) / Resolution: 11.6 Å

Source
  • Streptomyces venezuelae (bacteria)
  • unidentified (others)

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