6fik

ACP2 crosslinked to the KS of the loading/condensing region of the CTB1 PKSACP2 crosslinked to the KS of the loading/condensing region of the CTB1 PKS

6fik, resolution 7.10Å Show:Asymmetric Unit Biological Assembly Structural highlights 6fik is a 3 chain structure with sequence from Barn spot disease fungus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 6fij Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Polyketide synthases (PKSs) are microbial multienzymes for the biosynthesis of biologically potent secondary metabolites. Polyketide production is initiated by the loading of a starter unit onto an integral acyl carrier protein (ACP) and its subsequent transfer to the ketosynthase (KS). Initial substrate loading is achieved either by multidomain loading modules or by the integration of designated loading domains, such as starter unit acyltransferases (SAT), whose structural integration into PKS remains unresolved. A crystal structure of the loading/condensing region of the nonreducing PKS CTB1 demonstrates the ordered insertion of a pseudodimeric SAT into the condensing region, which is aided by the SAT-KS linker. Cryo-electron microscopy of the post-loading state trapped by mechanism-based crosslinking of ACP to KS reveals asymmetry across the CTB1 loading/-condensing region, in accord with preferential 1:2 binding stoichiometry. These results are critical for re-engineering the loading step in polyketide biosynthesis and support functional relevance of asymmetric conformations of PKSs. The structural organization of substrate loading in iterative polyketide synthases.,Herbst DA, Huitt-Roehl CR, Jakob RP, Kravetz JM, Storm PA, Alley JR, Townsend CA, Maier T Nat Chem Biol. 2018 Apr 2. pii: 10.1038/s41589-018-0026-3. doi:, 10.1038/s41589-018-0026-3. PMID:29610486 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.