The crystal structure of uncomplexed actin in the ADP state.
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.
Otterbein
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Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.
Graceffa
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Dominguez
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D000199:Actins / Q000737:chemistry* / Q000378:metabolism*; D000244:Adenosine Diphosphate / Q000737:chemistry / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D001704:Biopolymers / Q000737:chemistry / Q000378:metabolism; D002118:Calcium / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D003850:Deoxyribonuclease I / Q000378:metabolism; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010710:Phosphates / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012235:Rhodamines / Q000378:metabolism
D000199:Actins; D001704:Biopolymers; D010710:Phosphates; D012235:Rhodamines; D000244:Adenosine Diphosphate; C005358:tetramethylrhodamine; D000255:Adenosine Triphosphate; D003850:Deoxyribonuclease I; D002118:Calcium