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6QSP

Ketosynthase (ApeO) in Complex with its Chain Length Factor (ApeC) from Xenorhabdus doucetiae

Summary for 6QSP
Entry DOI10.2210/pdb6qsp/pdb
Related1TQY 2IWZ
DescriptorBeta-ketoacyl synthase, Uncharacterized protein, GLYCEROL, ... (5 entities in total)
Functional Keywordsaryl polyene pigment, biosynthesis, type ii polyketide synthase, ketoacyl synthase, chain elongation, claisen condensation, biosynthetic protein
Biological sourceXenorhabdus doucetiae
More
Total number of polymer chains2
Total formula weight70555.76
Authors
Grammbitter, G.L.C.,Schmalhofer, M.,Groll, M.,Bode, H. (deposition date: 2019-02-21, release date: 2019-04-03, Last modification date: 2024-01-24)
Primary citationGrammbitter, G.L.C.,Schmalhofer, M.,Karimi, K.,Shi, Y.M.,Schoner, T.A.,Tobias, N.J.,Morgner, N.,Groll, M.,Bode, H.B.
An Uncommon Type II PKS Catalyzes Biosynthesis of Aryl Polyene Pigments.
J.Am.Chem.Soc., 141:16615-16623, 2019
Cited by
PubMed Abstract: Aryl polyene (APE) pigments are a widely distributed class of bacterial polyketides. So far, little is known about the biosynthesis of these compounds, which are produced by a novel type II polyketide synthase (PKS). We have identified all enzymes involved in APE biosynthesis and determined their peculiar functions. The biosynthesis was reconstituted , and ACP-bound intermediates were assigned for each reaction step by HPLC-MS. Native mass spectrometry experiments identified four stable complexes: the acyl-carrier proteins ApeE and ApeF bound to the thioesterase ApeK, the dehydratases ApeI and ApeP, and the ketosynthase ApeO in complex with its chain-length factor ApeC. X-ray structures of the heterodimeric ApeO:ApeC and ApeI:ApeP complexes depict striking protein-protein interactions. Altogether, our study elucidated mechanistic aspects of APE biosynthesis that unifies elements of type II fatty acid and PKS systems, but in addition includes novel enzyme complexes.
PubMed: 30908039
DOI: 10.1021/jacs.8b10776
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.45 Å)
Structure validation

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