6QSR

The Dehydratase Heterocomplex ApeI:P from Xenorhabdus doucetiae

Summary for 6QSR

• Entry DOI: 10.2210/pdb6qsr/pdb
• Related: 3ESI
• Descriptor: AMP-dependent synthetase and ligase, Beta-hydroxyacyl-(Acyl-carrier-protein) dehydratase FabA/FabZ, SODIUM ION, ... (4 entities in total)
• Functional Keywords: aryl polyene pigment, biosynthesis, type ii polyketide synthase, dehydration, biosynthetic protein
• Biological source: Xenorhabdus doucetiae; More
• Total number of polymer chains: 2
• Total formula weight: 34243.09

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

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

Experimental method

X-RAY DIFFRACTION (1.85 Å)