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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Actins / chemistry*
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Actins / metabolism*
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Adenosine Diphosphate / chemistry
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Adenosine Diphosphate / metabolism*
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Adenosine Triphosphate / chemistry
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Adenosine Triphosphate / metabolism
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Binding Sites
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Biopolymers / chemistry
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Biopolymers / metabolism
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Calcium / metabolism
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Crystallization
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Crystallography, X-Ray
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Deoxyribonuclease I / metabolism
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Hydrogen Bonding
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Models, Molecular
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Phosphates / metabolism
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Protein Conformation
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Protein Folding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Rhodamines / metabolism
Substances
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Actins
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Biopolymers
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Phosphates
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Rhodamines
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Adenosine Diphosphate
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tetramethylrhodamine
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Adenosine Triphosphate
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Deoxyribonuclease I
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Calcium