The Crystal Structure of Uncomplexed Actin in the ADP State

  • Ludovic R. Otterbein
    Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.
  • Philip Graceffa
    Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.
  • Roberto Dominguez
    Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.

抄録

<jats:p>The dynamics and polarity of actin filaments are controlled by a conformational change coupled to the hydrolysis of adenosine 5′-triphosphate (ATP) by a mechanism that remains to be elucidated. Actin modified to block polymerization was crystallized in the adenosine 5′-diphosphate (ADP) state, and the structure was solved to 1.54 angstrom resolution. Compared with previous ATP-actin structures from complexes with deoxyribonuclease I, profilin, and gelsolin, monomeric ADP-actin is characterized by a marked conformational change in subdomain 2. The successful crystallization of monomeric actin opens the way to future structure determinations of actin complexes with actin-binding proteins such as myosin.</jats:p>

収録刊行物

  • Science

    Science 293 (5530), 708-711, 2001-07-27

    American Association for the Advancement of Science (AAAS)

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