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• W2059642562 endingPage "2245" @default.
• W2059642562 startingPage "2229" @default.
• W2059642562 abstract "The 6-deoxyerythronolide B synthase (DEBS) is a prototypical assembly line polyketide synthase produced by the actinomycete Saccharopolyspora erythraea that synthesizes the macrocyclic core of the antibiotic erythromycin 6-deoxyerythronolide B. The megasynthase is a 2-MDa trimeric complex composed of three unique homodimers assembled from the gene products DEBS1, DEBS2, and DEBS3, which are housed within the erythromycin biosynthetic gene cluster. Each homodimer contains two clusters of catalytically independent enzymatic domains, each referred to as a module, which catalyzes one round of polyketide chain extension and modification. Modules are named sequentially to indicate the order in which they are utilized during synthesis of 6-deoxyerythronolide B. We report small-angle X-ray scattering (SAXS) analyses of a whole module and a bimodule from DEBS, as well as a set of domains for which high-resolution structures are available. In all cases, the solution state was probed under previously established conditions ensuring that each protein is catalytically active. SAXS data are consistent with atomic-resolution structures of DEBS fragments. Therefore, we used the available high-resolution structures of DEBS domains to model the architectures of the larger protein assemblies using rigid-body refinement. Our data support a model in which the third module of DEBS forms a disc-shaped structure capable of caging the acyl carrier protein domain proximal to each active site. The molecular envelope of DEBS3 is a thin elongated ellipsoid, and the results of rigid-body modeling suggest that modules 5 and 6 stack collinearly along the 2-fold axis of symmetry." @default.
• W2059642562 created "2016-06-24" @default.
• W2059642562 creator A5009946597 @default.
• W2059642562 creator A5038399044 @default.
• W2059642562 creator A5047821642 @default.
• W2059642562 creator A5066394814 @default.
• W2059642562 date "2014-05-01" @default.
• W2059642562 modified "2023-10-12" @default.
• W2059642562 title "Architectures of Whole-Module and Bimodular Proteins from the 6-Deoxyerythronolide B Synthase" @default.
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• W2059642562 doi "https://doi.org/10.1016/j.jmb.2014.03.015" @default.
• W2059642562 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4284093" @default.
• W2059642562 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24704088" @default.
• W2059642562 hasPublicationYear "2014" @default.
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