8G4U

Final ketosynthase+acyltransferase of the erythromycin modular polyketide synthase

Summary for 8G4U

• Entry DOI: 10.2210/pdb8g4u/pdb
• Descriptor: EryAIII (2 entities in total)
• Functional Keywords: ketosynthase, acyltransferase, cerulenin, multimerization, biosynthetic protein
• Biological source: Saccharopolyspora erythraea
• Total number of polymer chains: 4
• Total formula weight: 363817.38

Authors

Keatinge-Clay, A.T. (deposition date: 2023-02-10, release date: 2023-03-01, Last modification date: 2024-05-22)

Primary citation

Keatinge-Clay, A.T.,Miyazawa, T.,Zhang, J.,Ray, K.A.,Lutgens, J.D.,Bista, R.,Lin, S.N.
Crystal structures reveal the framework of cis -acyltransferase modular polyketide synthases.
Biorxiv, 2023

PubMed Abstract: Although the domains of -acyltransferase ( -AT) modular polyketide synthases (PKS's) have been understood at atomic resolution for over a decade, the domain-domain interactions responsible for the architectures and activities of these giant molecular assembly lines remain largely uncharacterized. The multimeric structure of the α β fungal fatty acid synthase (FAS) provides 6 equivalent reaction chambers for its acyl carrier protein (ACP) domains to shuttle carbon building blocks and the growing acyl chain between surrounding, oriented enzymatic domains. The presumed homodimeric oligomerization of -AT assembly lines is insufficient to provide similar reaction chambers; however, the crystal structure of a ketosynthase (KS)+AT didomain presented here and three already reported show an interaction between the AT domains appropriate for lateral multimerization. This interaction was used to construct a framework for the pikromycin PKS from its KS, AT, and docking domains that contains highly-ordered reaction chambers. Its AT domains also mediate vertical interactions, both with upstream KS domains and downstream docking domains.

PubMed: 36798387
DOI: 10.1101/2023.02.11.528132

Experimental method

X-RAY DIFFRACTION (2.9 Å)