The Crystal Structure of Uncomplexed Actin in the ADP State

@article{Otterbein2001TheCS,
  title={The Crystal Structure of Uncomplexed Actin in the ADP State},
  author={Ludovic R. Otterbein and Philip Graceffa and Roberto 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… 

Crystal Structure of Monomeric Actin in the ATP State

The x-ray crystal structure of tetramethylrhodamine-5-maleimide-actin with bound AMPPNP, a non-hydrolyzable ATP analog, was determined and an analysis of the existing structures of members of the actin superfamily suggests that the cleft is open in the nucleotide-free state.

ATPase activity and conformational changes in the regulation of actin.

  • H. Schüler
  • Chemistry, Biology
    Biochimica et biophysica acta
  • 2001

Structure and dynamics of the actin filament.

Bound nucleotide can control the dynamic architecture of monomeric actin

A model in which differential sampling of a nucleation-compatible form of the actin monomer may contribute to control of actin filament dynamics by nucleotide is suggested.

Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM

Six high-resolution cryo-EM structures of F-actin from rabbit skeletal muscle in different nucleotide states reveal that actin polymerization repositions the proposed catalytic base, His161, closer to the γ-phosphate.

Effects of Nucleotide and End-Dependent Actin Conformations on Polymerization.

ATP and ADP actin states.

It is concluded that the existing evidence points to dynamic equilibria of these structural elements among various conformational states in both ATP- and ADP-actins, with the nucleotides impacting theEquilibria distributions.

Nucleotide effects on the structure and dynamics of actin.

Structural differences in the nucleotide binding cleft provide a structural basis for understanding the observed differences between the various nucleotide states of actin and provide some insight into how ATP regulates the interaction of act in with itself and other proteins.

Crystal Structures of Expressed Non-polymerizable Monomeric Actin in the ADP and ATP States*

This work expressed a cytoplasmic actin in Sf9 cells, which was rendered non-polymerizable by virtue of two point mutations in subdomain 4 (A204E/P243K), and suggests that the nucleotide-dependent formation of the D-loop helix may result from signal propagation through crystal packing interactions.

Nucleotide-dependent conformational changes in the actin filament: Subtler than expected

  • R. Dominguez
  • Chemistry
    Proceedings of the National Academy of Sciences
  • 2019
Crystallization has been made possible using one of several strategies that prevent polymerization, including mutagenesis, covalent modification of actin, and the formation of soluble complexes with actin-binding protein (ABPs) or marine toxins.
...

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