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The Crystal Structure of Uncomplexed Actin in the ADP State

2001/07/27 by Ludovic R. Otterbein, Philip Graceffa, Roberto Domínguez · 14 citations
Biochemistry, Genetics and Molecular Biology · Medicine · Neuroscience · Chemistry · #Cellular Mechanics and Interactions #Cardiomyopathy and Myosin Studies #Genetic Neurodegenerative Diseases #Actin #Chemistry #Gelsolin #Biophysics #ATP hydrolysis #Adenosine triphosphate #Deoxyribonuclease I #Adenosine diphosphate #Myosin #Actin remodeling #Conformational change #Monomer #Biochemistry #Cytoskeleton #Polymer #Actin cytoskeleton #Platelet aggregation #Biology #ATPase #DNA #Cell #Enzyme #Platelet

paper · doi:10.1126/science.1059700

openalex publication_date 2001/07/27 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01

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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