6QSP
Ketosynthase (ApeO) in Complex with its Chain Length Factor (ApeC) from Xenorhabdus doucetiae
Summary for 6QSP
| Entry DOI | 10.2210/pdb6qsp/pdb |
| Related | 1TQY 2IWZ |
| Descriptor | Beta-ketoacyl synthase, Uncharacterized protein, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | aryl polyene pigment, biosynthesis, type ii polyketide synthase, ketoacyl synthase, chain elongation, claisen condensation, biosynthetic protein |
| Biological source | Xenorhabdus doucetiae More |
| Total number of polymer chains | 2 |
| Total formula weight | 70555.76 |
| 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 citation | Grammbitter, 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: 30908039DOI: 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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