Structural Biology

A domain swap makes motor rings

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Science  25 Mar 2016:
Vol. 351, Issue 6280, pp. 1412
DOI: 10.1126/science.351.6280.1412-b

Cells are packed with protein complexes. Cells must appropriately assemble these complexes while ensuring that component proteins do not aggregate prematurely. Baker et al. show that the FliG protein, part of the bacterial flagellar motor complex, can polymerize to forms rings by “domain swapping.” Domains within a single FliG can interact with each other or “swap” with neighboring FliG proteins to form the same interaction—a molecular form of linking arms. The flexibility of the peptides that tether these domains ensures that FliG remains a monomer in the cytoplasm. FliG binding to a scaffolding ring promotes motor assembly by increasing the local concentration of FliG and promoting domain swapping.

Nat. Struct. Mol. Biol. 197, 23 (2016).

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