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Science. 2001 Jul 27;293(5530):616-8.
The crystal structure of uncomplexed actin in the ADP state.
Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.
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.
PMID: 11474115 [PubMed - indexed for MEDLINE]