8RAJ

NMR structure of PKS docking domains

Summary for 8RAJ

• Entry DOI: 10.2210/pdb8raj/pdb
• NMR Information: BMRB: 34886
• Descriptor: Beta-ketoacyl synthase, Trimethylamine monooxygenase (2 entities in total)
• Functional Keywords: docking domain, polyketide synthase, protein binding
• Biological source: Methylorubrum extorquens AM1; More
• Total number of polymer chains: 2
• Total formula weight: 11676.80

Authors

Scat, S.,Weissman, K.J.,Chagot, B. (deposition date: 2023-12-01, release date: 2024-06-05, Last modification date: 2024-07-17)

Primary citation

Scat, S.,Weissman, K.J.,Chagot, B.
Insights into docking in megasynthases from the investigation of the toblerol trans -AT polyketide synthase: many alpha-helical means to an end.
Rsc Chem Biol, 5:669-683, 2024

PubMed Abstract: The fidelity of biosynthesis by modular polyketide synthases (PKSs) depends on specific moderate affinity interactions between successive polypeptide subunits mediated by docking domains (DDs). These sequence elements are notably portable, allowing their transplantation into alternative biosynthetic and metabolic contexts. Herein, we use integrative structural biology to characterize a pair of DDs from the toblerol -AT PKS. Both are intrinsically disordered regions (IDRs) that fold into a 3 α-helix docking complex of unprecedented topology. The C-terminal docking domain (DD) resembles the 4 α-helix type (4HB) DDs, which shows that the same type of DD can be redeployed to form complexes of distinct geometry. By carefully re-examining known DD structures, we further extend this observation to type 2 docking domains, establishing previously unsuspected structural relations between DD types. Taken together, these data illustrate the plasticity of α-helical DDs, which allow the formation of a diverse topological spectrum of docked complexes. The newly identified DDs should also find utility in modular PKS genetic engineering.

PubMed: 38966669
DOI: 10.1039/d4cb00075g

Experimental method

SOLUTION NMR