8G7W
Type I modPKS reducing region
Summary for 8G7W
| Entry DOI | 10.2210/pdb8g7w/pdb |
| Descriptor | Type I PKS module 4, module 5, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | polyketide synthase, reducing region, modpks, biosynthetic protein |
| Biological source | Micromonospora chalcea subsp. izumensis |
| Total number of polymer chains | 2 |
| Total formula weight | 221705.84 |
| Authors | McCullough, T.M.,Smith, J.L. (deposition date: 2023-02-17, release date: 2023-06-07, Last modification date: 2023-09-20) |
| Primary citation | McCullough, T.M.,Dhar, A.,Akey, D.L.,Konwerski, J.R.,Sherman, D.H.,Smith, J.L. Structure of a modular polyketide synthase reducing region. Structure, 31:1109-1120.e3, 2023 Cited by PubMed Abstract: The chemical scaffolds of numerous therapeutics are polyketide natural products, many formed by bacterial modular polyketide synthases (PKS). The large and flexible dimeric PKS modules have distinct extension and reducing regions. Structures are known for all individual enzyme domains and several extension regions. Here, we report the structure of the full reducing region from a modular PKS, the ketoreductase (KR), dehydratase (DH), and enoylreductase (ER) domains of module 5 of the juvenimicin PKS. The modular PKS-reducing region has a different architecture than the homologous fatty acid synthase (FAS) and iterative PKS systems in its arrangement of domains and dimer interface. The structure reveals a critical role for linker peptides in the domain interfaces, leading to discovery of key differences in KR domains dependent on module composition. Finally, our studies provide insight into the mechanism underlying modular PKS intermediate shuttling by carrier protein (ACP) domains. PubMed: 37348494DOI: 10.1016/j.str.2023.05.019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
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