Abstract
TRANSCRIPTION of the ant gene during lytic growth of bacteriophage P22 (ref. 1) is regulated by the cooperative binding of two Arc repressor dimers to a 21-base-pair operator site2,3. Here we report the co-crystal structure of this Arc tetramer–operator complex at 2.6 Å resolution. As expected from genetic4–6 and structural studies7 and from the co-crystal structure of the homologous Escherichia coli MetJ repressor8, each Arc dimer uses an antiparallel ß-sheet to recognize bases in the major groove. However, the Arc and Met J complexes differ in several important ways: the (β-sheet–DNA interactions of Arc are far less symmetrical; DNA binding by Arc is accompanied by important conformational changes in the β-sheet; and Arc uses a different part of its protein surface for dimer–dimer interactions.
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Raumann, B., Rould, M., Pabo, C. et al. DNA recognition by β-sheets in the Arc represser–operator crystal structure. Nature 367, 754–757 (1994). https://doi.org/10.1038/367754a0
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DOI: https://doi.org/10.1038/367754a0
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