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TitlePriming enzymes from the pikromycin synthase reveal how assembly-line ketosynthases catalyze carbon-carbon chemistry.
Journal, issue, pagesStructure, Vol. 30, Issue 9, Page 1331-11339.e3, Year 2022
Publish dateSep 1, 2022
AuthorsMiles S Dickinson / Takeshi Miyazawa / Ryan S McCool / Adrian T Keatinge-Clay /
PubMed AbstractThe first domain of modular polyketide synthases (PKSs) is most commonly a ketosynthase (KS)-like enzyme, KS, that primes polyketide synthesis. Unlike downstream KSs that fuse α-carboxyacyl groups ...The first domain of modular polyketide synthases (PKSs) is most commonly a ketosynthase (KS)-like enzyme, KS, that primes polyketide synthesis. Unlike downstream KSs that fuse α-carboxyacyl groups to growing polyketide chains, it performs an extension-decoupled decarboxylation of these groups to generate primer units. When Pik127, a model triketide synthase constructed from modules of the pikromycin synthase, was studied by cryoelectron microscopy (cryo-EM), the dimeric didomain comprised of KS and the neighboring methylmalonyl-selective acyltransferase (AT) dominated the class averages and yielded structures at 2.5- and 2.8-Å resolution, respectively. Comparisons with ketosynthases complexed with their substrates revealed the conformation of the (2S)-methylmalonyl-S-phosphopantetheinyl portion of KS and KS substrates prior to decarboxylation. Point mutants of Pik127 probed the roles of residues in the KS active site, while an AT-swapped version of Pik127 demonstrated that KS can also decarboxylate malonyl groups. Mechanisms for how KS and KS domains catalyze carbon-carbon chemistry are proposed.
External linksStructure / PubMed:35738283 / PubMed Central
MethodsEM (single particle)
Resolution2.61 - 2.86 Å
Structure data

26839

7uwr

EMDB-26839, PDB-7uwr:
KSQ+AT from first module of the pikromycin synthase
Method: EM (single particle) / Resolution: 2.61 Å

27094

8czc

EMDB-27094, PDB-8czc:
AT from first module of the pikromycin synthase
Method: EM (single particle) / Resolution: 2.86 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • streptomyces venezuelae (bacteria)
KeywordsBIOSYNTHETIC PROTEIN / ketosynthase-like / acyltransferase / decarboxylation / methylmalonyl-specific / polyketide synthase

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