8A82

Fe(II)/aKG-dependent halogenase OocPQ

Summary for 8A82

• Entry DOI: 10.2210/pdb8a82/pdb
• Descriptor: Cupin_8 domain-containing protein, OocQ, FE (III) ION, ... (5 entities in total)
• Functional Keywords: halogenase, polyketide synthase, biosynthesis, metal catalysis, biosynthetic protein
• Biological source: Serratia plymuthica 4Rx13; More
• Total number of polymer chains: 2
• Total formula weight: 59412.31

Authors

Fraley, A.E.,Meoded, R.A.,Schmalhofer, M.,Bergande, C.,Groll, M.,Piel, J. (deposition date: 2022-06-21, release date: 2023-03-08, Last modification date: 2024-06-19)

Primary citation

Fraley, A.E.,Dell, M.,Schmalhofer, M.,Meoded, R.A.,Bergande, C.,Groll, M.,Piel, J.
Heterocomplex structure of a polyketide synthase component involved in modular backbone halogenation.
Structure, 31:565-, 2023

PubMed Abstract: Bacterial modular polyketide synthases (PKSs) generate diverse, complex and bioactive natural products that are constructed mainly based on principles of fatty acid biosynthesis. The cytotoxic oocydin-type polyketides contain a vinyl chloride moiety introduced during polyketide chain elongation. Required for modular polyketide backbone halogenation are a non-heme iron and ɑ-ketoglutarate-dependent halogenase OocP and OocQ lacking characterized homologs. This work provides structural insights into these unusual PKS components and their interactions via a high-resolution X-ray crystallography structure of the heterocomplex. By mapping the protein-protein interactions and comparison with structures of similar halogenases, we illustrate the potential of this heterodimer complex as a replacement for the conserved homodimeric structure of homologous enzymes. The OocPQ protein pair has thus evolved as a means of stabilizing the halogenase and facilitating chemical transformations with great synthetic utility.

PubMed: 36917986
DOI: 10.1016/j.str.2023.02.010

Experimental method

X-RAY DIFFRACTION (2.05 Å)