5MPT
Structure of the citrinin polyketide synthase CMeT domain
Summary for 5MPT
| Entry DOI | 10.2210/pdb5mpt/pdb |
| Descriptor | Citrinin polyketide synthase, S-ADENOSYL-L-HOMOCYSTEINE, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | pks, polyketide, natural product, domain deconstruction, citrinin, c-methylation, methyltransferase, transferase |
| Biological source | Monascus purpureus |
| Total number of polymer chains | 1 |
| Total formula weight | 47268.19 |
| Authors | Herbst, D.A.,Storm, P.A.,Townsend, C.A.,Maier, T. (deposition date: 2016-12-19, release date: 2017-02-22, Last modification date: 2025-12-10) |
| Primary citation | Storm, P.A.,Herbst, D.A.,Maier, T.,Townsend, C.A. Functional and Structural Analysis of Programmed C-Methylation in the Biosynthesis of the Fungal Polyketide Citrinin. Cell Chem Biol, 24:316-325, 2017 Cited by PubMed Abstract: Fungal polyketide synthases (PKSs) are large, multidomain enzymes that biosynthesize a wide range of natural products. A hallmark of these megasynthases is the iterative use of catalytic domains to extend and modify a series of enzyme-bound intermediates. A subset of these iterative PKSs (iPKSs) contains a C-methyltransferase (CMeT) domain that adds one or more S-adenosylmethionine (SAM)-derived methyl groups to the carbon framework. Neither the basis by which only specific positions on the growing intermediate are methylated ("programming") nor the mechanism of methylation are well understood. Domain dissection and reconstitution of PksCT, the fungal non-reducing PKS (NR-PKS) responsible for the first isolable intermediate in citrinin biosynthesis, demonstrates the role of CMeT-catalyzed methylation in precursor elongation and pentaketide formation. The crystal structure of the S-adenosyl-homocysteine (SAH) coproduct-bound PksCT CMeT domain reveals a two-subdomain organization with a novel N-terminal subdomain characteristic of PKS CMeT domains and provides insights into co-factor and ligand recognition. PubMed: 28238725DOI: 10.1016/j.chembiol.2017.01.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.648 Å) |
Structure validation
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