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|1pzq, 8 NMR models ()|
|Gene:||ERYA (Saccharopolyspora erythraea)|
Structure of fused docking domains from the erythromycin polyketide synthase (DEBS), a model for the interaction between DEBS 2 and DEBS 3: The A domain
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Broadhurst RW, Nietlispach D, Wheatcroft MP, Leadlay PF, Weissman KJ. The structure of docking domains in modular polyketide synthases. Chem Biol. 2003 Aug;10(8):723-31. PMID:12954331
- Sherman DH, Smith JL. Clearing the skies over modular polyketide synthases. ACS Chem Biol. 2006 Sep 19;1(8):505-9. PMID:17168537 doi:10.1021/cb600376r