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. 2001 Jul 27;293(5530):708-11.
doi: 10.1126/science.1059700.

The crystal structure of uncomplexed actin in the ADP state

L R Otterbein  1 , P Graceffa, R Dominguez
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The crystal structure of uncomplexed actin in the ADP state

L R Otterbein et al. Science. .

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.

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Comment in

  • Structural biology. Actin' up.
    De La Cruz EM, Pollard TD. De La Cruz EM, et al. Science. 2001 Jul 27;293(5530):616-8. doi: 10.1126/science.1063558. Science. 2001. PMID: 11474090 No abstract available.

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