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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References
Susskind, M. & Youderian, P. in Lambda II (eds Hendrix, R. W., Roberts, J. W., Stahl, F. W. & Weisberg, R. A.) 347–364 (Cold Spring Harbor Laboratory, New York, 1983).
Vershon, A. K., Liao, S. M., McClure, W. R. & Sauer, R. T. J. molec. Biol. 195, 323–331 (1987).
Brown, B. M. & Sauer, R. T. Biochemistry 32, 1354–1363 (1993).
Knight, K. L. & Sauer, R. T. Proc. natn. Acad. Sci. U.S.A. 86, 797–801 (1989).
Bowie, J. U. & Sauer, R. T. Proc. natn. Acad. Sci. U.S.A. 86, 2152–2156 (1989).
Vershon, A. K., Bowie, J. U., Karplus, T. M. & Sauer, R. T. Proteins 1, 302–311 (1986).
Breg, J. N., van Opheusden, J. H. J., Burgering, M. J., Boelens, R. & Kaptein, R. Nature 346, 586–589 (1990).
Somers, W. S. & Phillips, S. E. Nature 359, 387–393 (1992).
Vershon, A. K., Kelley, R. D. & Sauer, R. T. J. biol. Chem. 264, 3267–3273 (1989).
Brown, B. M., Bowie, J. U. & Sauer, R. T. Biochemistry 29, 11189–11195 (1990).
Brown, B. M., Milla, M. E., Smith, T. L. & Sauer, R. T. Nature struct. Biol. (in the press).
Saenger, W. Principles of Nucleic Acid Structure (Springer, New York, 1984).
Phillips, S. E. V. Curr. Opin. struct Biol. 1, 89–98 (1991).
SERC [UK] Collaborative Computing Project No. 4 (Daresbury Laboratory, Warrington, UK, 1979).
Jones, T. A. J. appl. Crystallogr. 11, 268–272 (1978).
Brunger, A. T., Kuriyan, J. & Karplus, M. Science 235, 458–460 (1987).
Brunger, A. T. X-PLOR v3.1 Manual (Yale Univ. Press, New Haven, 1992).
Tronrud, D. E., Ten Eyck, L. F. & Matthews, B. W. Acta crystallogr. 43, 489–501 (1987).
Ravishanker, G., Swaminathan, S., Beveridge, D. L., Lavery, R. & Sklenar, H. J. Biomolec. struct. Dyn. 6, 669–699 (1989).
Lavery, R. & Sklenar, H. J. biomolec. str. Dyn. 6, 63–91 (1988).
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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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