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TitleStructure of a modular polyketide synthase.
Journal, issue, pagesNature, Vol. 510, Issue 7506, Page 512-517, Year 2014
Publish dateJun 26, 2014
AuthorsSomnath Dutta / Jonathan R Whicher / Douglas A Hansen / Wendi A Hale / Joseph A Chemler / Grady R Congdon / Alison R H Narayan / Kristina Håkansson / David H Sherman / Janet L Smith / Georgios Skiniotis /
PubMed AbstractPolyketide natural products constitute a broad class of compounds with diverse structural features and biological activities. Their biosynthetic machinery, represented by type I polyketide synthases ...Polyketide natural products constitute a broad class of compounds with diverse structural features and biological activities. Their biosynthetic machinery, represented by type I polyketide synthases (PKSs), has an architecture in which successive modules catalyse two-carbon linear extensions and keto-group processing reactions on intermediates covalently tethered to carrier domains. Here we used electron cryo-microscopy to determine sub-nanometre-resolution three-dimensional reconstructions of a full-length PKS module from the bacterium Streptomyces venezuelae that revealed an unexpectedly different architecture compared to the homologous dimeric mammalian fatty acid synthase. A single reaction chamber provides access to all catalytic sites for the intramodule carrier domain. In contrast, the carrier from the preceding module uses a separate entrance outside the reaction chamber to deliver the upstream polyketide intermediate for subsequent extension and modification. This study reveals for the first time, to our knowledge, the structural basis for both intramodule and intermodule substrate transfer in polyketide synthases, and establishes a new model for molecular dissection of these multifunctional enzyme systems.
External linksNature / PubMed:24965652 / PubMed Central
MethodsEM (single particle)
Resolution7.3 - 12.5 Å
Structure data

EMDB-5647:
Cryo-EM structure of holo-PikAIII conformation 1
Method: EM (single particle) / Resolution: 9.2 Å

EMDB-5648:
Cryo-EM structure of holo-PikAIII conformation 2
Method: EM (single particle) / Resolution: 9.5 Å

EMDB-5649:
Cryo-EM structure of PikAIII/delta ACP5
Method: EM (single particle) / Resolution: 7.8 Å

EMDB-5651:
Cryo-EM structure pentaketide-ACP4-PikAIII/C209A/delta ACP5
Method: EM (single particle) / Resolution: 8.6 Å

EMDB-5653:
Cryo-EM structure of MeMal-PikAIII
Method: EM (single particle) / Resolution: 7.3 Å

EMDB-5662:
holo-ACP4-PikAIII/C209A/delta ACP5 (no pentaketide)
Method: EM (single particle) / Resolution: 12.5 Å

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

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