2N5D

NMR structure of PKS domains

Summary for 2N5D

• Entry DOI: 10.2210/pdb2n5d/pdb
• NMR Information: BMRB: 25706
• Descriptor: fusion protein of two PKS domains (1 entity in total)
• Functional Keywords: docking domain, polyketide synthase, protein binding
• Biological source: Streptomyces virginiae
• Total number of polymer chains: 1
• Total formula weight: 8455.41

Authors

Dorival, J.,Annaval, T.,Risser, F.,Collin, S.,Roblin, P.,Jacob, C.,Gruez, A.,Chagot, B.,Weissman, K.J. (deposition date: 2015-07-14, release date: 2016-03-23, Last modification date: 2024-05-15)

Primary citation

Dorival, J.,Annaval, T.,Risser, F.,Collin, S.,Roblin, P.,Jacob, C.,Gruez, A.,Chagot, B.,Weissman, K.J.
Characterization of Intersubunit Communication in the Virginiamycin trans-Acyl Transferase Polyketide Synthase.
J.Am.Chem.Soc., 138:4155-4167, 2016

PubMed Abstract: Modular polyketide synthases (PKSs) direct the biosynthesis of clinically valuable secondary metabolites in bacteria. The fidelity of chain growth depends on specific recognition between successive subunits in each assembly line: interactions mediated by C- and N-terminal "docking domains" (DDs). We have identified a new family of DDs in trans-acyl transferase PKSs, exemplified by a matched pair from the virginiamycin (Vir) system. In the absence of C-terminal partner (VirA (C)DD) or a downstream catalytic domain, the N-terminal DD (VirFG (N)DD) exhibits multiple characteristics of an intrinsically disordered protein. Fusion of the two docking domains results in a stable fold for VirFG (N)DD and an overall protein-protein complex of unique topology whose structure we support by site-directed mutagenesis. Furthermore, using small-angle X-ray scattering (SAXS), the positions of the flanking acyl carrier protein and ketosynthase domains have been identified, allowing modeling of the complete intersubunit interface.

PubMed: 26982529
DOI: 10.1021/jacs.5b13372

Experimental method

SOLUTION NMR