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Science 27 July 2001:
Vol. 293. no. 5530, pp. 708 - 711
DOI: 10.1126/science.1059700
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Reports

The Crystal Structure of Uncomplexed Actin in the ADP State

Ludovic R. Otterbein, Philip Graceffa, Roberto Dominguez*

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.

Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.
*   To whom correspondence should be addressed. E-mail: dominguez{at}bbri.org

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