7ZM9
Ketosynthase domain 3 of Brevibacillus Brevis orphan BGC11
Summary for 7ZM9
| Entry DOI | 10.2210/pdb7zm9/pdb |
| Descriptor | Putative polyketide synthase, DI(HYDROXYETHYL)ETHER, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | ketosynthase, polyketide synthase, claisen condensation, thiolase fold, biosynthetic protein |
| Biological source | Brevibacillus brevis NBRC 100599 |
| Total number of polymer chains | 1 |
| Total formula weight | 68048.50 |
| Authors | Tittes, Y.U.,Herbst, D.A.,Jakob, R.P.,Maier, T. (deposition date: 2022-04-19, release date: 2022-09-21, Last modification date: 2024-11-20) |
| Primary citation | Tittes, Y.U.,Herbst, D.A.,Martin, S.F.X.,Munoz-Hernandez, H.,Jakob, R.P.,Maier, T. The structure of a polyketide synthase bimodule core. Sci Adv, 8:eabo6918-eabo6918, 2022 Cited by PubMed Abstract: Polyketide synthases (PKSs) are predominantly microbial biosynthetic enzymes. They assemble highly potent bioactive natural products from simple carboxylic acid precursors. The most versatile families of PKSs are organized as assembly lines of functional modules. Each module performs one round of precursor extension and optional modification, followed by directed transfer of the intermediate to the next module. While enzymatic domains and even modules of PKSs are well understood, the higher-order modular architecture of PKS assembly lines remains elusive. Here, we visualize a PKS bimodule core using cryo-electron microscopy and resolve a two-dimensional meshwork of the bimodule core formed by homotypic interactions between modules. The sheet-like organization provides the framework for efficient substrate transfer and for sequestration of trans-acting enzymes required for polyketide production. PubMed: 36129979DOI: 10.1126/sciadv.abo6918 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.62 Å) |
Structure validation
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