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Structure and mobility of the PUT3 dimer

Nature Structural Biology volume 4, pages 744750 (1997) | Download Citation

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Abstract

The solution structure and backbone dynamics of the transcriptional activator PUTS (31–100) has been characterized using NMR spectroscopy. PUT3 (31–100) contains three distinct domains: a cysteine zinc cluster, linker, and dimerization domain. The cysteine zinc cluster of PUT3 closely resembles the solution structure of GAL4, while the dimerization domain forms a long coiled-coil similar to that observed in the crystal structures of GAL4 and PPR1. However, the residues at the N-terminal end of the coiled-coil behave very differently in each of these proteins. A comparison of the structural elements within this region provides a model for the DMA binding specificity of these proteins. Furthermore, we have characterized the dynamics of PUT3 to find that the zinc cluster and dimerization domains have very diverse dynamics in solution. The dimerization domain behaves as a large protein, while the peripheral cysteine zinc clusters have dynamic properties similar to small proteins.

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Affiliations

  1. Committee on Higher Degrees in Biophysics, Harvard University, Cambridge, Massachusetts 02138 and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.

    • Kylie J. Walters
    •  & Gerhard Wagner
  2. MIT Chemistry Department, 77 Massachusetts Ave. Building 56-546, Cambridge, Massachusetts 02139, USA

    • Kwaku T. Dayie
  3. School of Biological Science, 2.205 Stopford Building, University of Manchester, Oxford Road, Manchester M13 9PT, UK.

    • Richard J. Reece
  4. Department of Cellular and Developmental Biology, Harvard University, Cambridge, Massachusetts 02138, USA.

    • Mark Ptashne
  5. wdgnei@wagner.med.harvard.edu

    • Gerhard Wagner

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https://doi.org/10.1038/nsb0997-744

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