1pzr
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Structure of fused docking domains from the erythromycin polyketide synthase (DEBS), a model for the interaction between DEBS2 and DEBS3: the B domain
OverviewOverview
Polyketides from actinomycete bacteria provide the basis for many valuable, medicines, so engineering genes for their biosynthesis to produce variant, molecules holds promise for drug discovery. The modular polyketide, synthases are particularly amenable to this approach, because each cycle, of chain extension is catalyzed by a different module of enzymes, and the, modules are arranged within giant multienzyme subunits in the order in, which they act. Protein-protein interactions between terminal docking, domains of successive multienzymes promote their correct positioning, within the assembly line, but because the overall complex is not stable in, vitro, the key interactions have not been identified. We present here the, NMR solution structure of a 120 residue polypeptide representing a typical, pair of such domains, fused at their respective C and N termini: it adopts, a stable dimeric structure which reveals the detailed role of these, (predominantly helical) domains in docking and dimerization by modular, polyketide synthases.
About this StructureAbout this Structure
1PZR is a Single protein structure of sequence from Saccharopolyspora erythraea. Active as Erythronolide synthase, with EC number 2.3.1.94 Full crystallographic information is available from OCA.
ReferenceReference
The structure of docking domains in modular polyketide synthases., Broadhurst RW, Nietlispach D, Wheatcroft MP, Leadlay PF, Weissman KJ, Chem Biol. 2003 Aug;10(8):723-31. PMID:12954331
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