7ZMF

Dehydratase domain of module 3 from Brevibacillus Brevis orphan BGC11

Summary for 7ZMF

• Entry DOI: 10.2210/pdb7zmf/pdb
• Descriptor: Putative polyketide synthase, MAGNESIUM ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: dehydratase, polyketide synthase, double hot dog fold, biosynthetic protein
• Biological source: Brevibacillus brevis NBRC 100599
• Total number of polymer chains: 2
• Total formula weight: 66996.35

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: 2024-02-07)

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

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: 36129979
DOI: 10.1126/sciadv.abo6918

Experimental method

X-RAY DIFFRACTION (2.21 Å)