2n5d | pdb_00002n5d

NMR structure of PKS domains

spinqualitylabelsall models 2n5d Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2n5d is a 1 chain structure with sequence from Streptomyces virginiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A4PHN0_STRVG Publication Abstract from PubMed 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 CDD) or a downstream catalytic domain, the N-terminal DD (VirFG NDD) 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. Characterization of Intersubunit Communication in the Virginiamycin trans-Acyl Transferase Polyketide Synthase.,Dorival J, Annaval T, Risser F, Collin S, Roblin P, Jacob C, Gruez A, Chagot B, Weissman KJ J Am Chem Soc. 2016 Mar 16. PMID:26982529 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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