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Characterization of Intersubunit Communication in the Virginiamycin trans-Acyl Transferase Polyketide Synthase

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 (DD)-D-C) or a downstream catalytic domain, the N-terminal DD (VirFG (DD)-D-N) exhibits multiple characteristics of an intrinsically disordered protein. Fusion of the two docking domains results in a stable fold for VirFG NDD 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.
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https://hal.univ-lorraine.fr/hal-01452317
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Submitted on : Wednesday, February 1, 2017 - 5:56:28 PM
Last modification on : Thursday, June 10, 2021 - 4:36:03 PM

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Jonathan Dorival, Thibault Annaval, Fanny Risser, Sabrina Collin, Pierre Roblin, et al.. Characterization of Intersubunit Communication in the Virginiamycin trans-Acyl Transferase Polyketide Synthase. Journal of the American Chemical Society, American Chemical Society, 2016, 138 (12), pp.4155-4167. ⟨10.1021/jacs.5b13372⟩. ⟨hal-01452317⟩

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