The Crystal Structure of Uncomplexed Actin in the ADP State

@article{Otterbein2001TheCS,
  title={The Crystal Structure of Uncomplexed Actin in the ADP State},
  author={L. Otterbein and P. Graceffa and R. Dominguez},
  journal={Science},
  year={2001},
  volume={293},
  pages={708 - 711}
}
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… Expand
Crystal Structure of Monomeric Actin in the ATP State
ATPase activity and conformational changes in the regulation of actin.
  • H. Schüler
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 2001
Structure and dynamics of the actin filament.
Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM
Effects of Nucleotide and End-Dependent Actin Conformations on Polymerization.
ATP and ADP actin states.
Nucleotide effects on the structure and dynamics of actin.
Nucleotide-dependent conformational changes in the actin filament: Subtler than expected
  • R. Dominguez
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences
  • 2019
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