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The Crystal Structure of Uncomplexed Actin in the ADP State

Science  27 Jul 2001:
Vol. 293, Issue 5530, pp. 708-711
DOI: 10.1126/science.1059700

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Abstract

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.

  • * To whom correspondence should be addressed. E-mail: dominguez{at}bbri.org

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