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Structure of a replication-terminator protein complexed with DNA

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Abstract

The crystal structure of the Escherichia colireplication-terminator protein (Tus) bound to terminus-site (Ter) DNA has been determined at 2.7 Å resolution. The Tus protein folds into a previously undescribed architecture divided into two domains by a central basic cleft. This cleft accommodates locally deformed B-form Ter DNA and makes extensive contacts with the major groove, mainly through two interdomain β-strands. The unusual structural features of this complex may explain how the replication fork is halted in only one direction.

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Authors and Affiliations

  1. Department of Genetics, The Graduate University for Advanced Studies, and National Institute of Genetics, 1111, Yata, Mishima, Shizuoka, 411, Japan

    Katsuhiko Kamada & Nobuo Shimamoto

  2. Protein Engineering Research Institute (Biomolecular Engineering Research Institute)§, 6-2-3, Furuedai, Suita, Osaka, 565, Japan

    Katsuhiko Kamada & Kosuke Morikawa

  3. Department of Molecular Biomechanics, The Graduate University for Advanced Studies, and National Institute for Basic Biology, 38, Nishigonaka, Myodaiji, Okazaki, Aichi, 444, Japan

    Takashi Horiuchi & Katsufumi Ohsumi

Authors
  1. Katsuhiko Kamada
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  2. Takashi Horiuchi
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  3. Katsufumi Ohsumi
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  4. Nobuo Shimamoto
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  5. Kosuke Morikawa
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Kamada, K., Horiuchi, T., Ohsumi, K. et al. Structure of a replication-terminator protein complexed with DNA. Nature 383, 598–603 (1996). https://doi.org/10.1038/383598a0

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  • DOI: https://doi.org/10.1038/383598a0

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