Research Article

Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility

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Science  08 Nov 2019:
Vol. 366, Issue 6466, eaaw4388
DOI: 10.1126/science.aaw4388

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Moving modules drive biosynthesis

Modular biosynthesis of small molecules—where enzyme units can be swapped in and out of assembly line complexes to produce desired products—is a distant goal in the lab despite a huge diversity of modular systems in nature. Part of the challenge is in understanding how modules interact and hand off intermediates. Reimer et al. determined crystal structures of portions of a nonribosomal peptide synthetase, including a full dimodule. Module positioning differed between these structures even when the same intermediate was attached to the enzyme. The authors used small-angle x-ray scattering to confirm that large conformational changes are possible during biosynthesis and handoff between modules.

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