The Crystal Structure of Uncomplexed Actin in the ADP State

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

NMR shows that ATP- and ADP-actin differ globally, including ground and excited state structures and dynamic architecture, andalyses of an actin mutant suggest the high-energy conformer of ATP- actin may be on the pathway to filament nucleation.

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.

Structural insights into actin-binding, branching and bundling proteins.

  • S. Winder
  • Biology, Chemistry
    Current opinion in cell biology
  • 2003

Atomic structure of the actin: DNase I complex

The atomic models of the complex between rabbit skeletal muscle actin and bovine pancreatic deoxyribonuclease I both in the ATP and ADP forms have been determined byo X-ray analysis at an effective

A conformational change in the actin subunit can change the flexibility of the actin filament.

It is determined that actin can exist in a state that has a fourfold increase in flexibility over normal F-actin, and nucleotide, which arises from a rotation of subdomain-2, the smallest subdomain, of the actin subunit.

The structure of crystalline profilin–β-actin

The three-dimensional structure of bovine profilin–β-actin has been solved to 2.55 Å resolution by X-ray crystallography and appears to correspond to the solution contact in vitro.

A change in actin conformation associated with filament instability after Pi release.

A yeast actin mutation is identified, Val-159 to Asn, which uncouples Pi release from the conformational change that results in filament destabilization, and it is proposed that these two conformations of G-actin may be related to two functional states of F-Actin.

Structure of gelsolin segment 1-actin complex and the mechanism of filament severing

The structure of the segment 1 domain of gelsolin, a protein that fragments actin filaments in cells, is reported in complex with actin, providing a basis for understanding the origin of an amyloidosis caused by a gelsolini variant.

Domain movement in gelsolin: a calcium-activated switch.

The 3.4 angstrom x-ray structure of the carboxyl-terminal half of gelsolin (G4-G6) in complex with actin reveals the basis for gelsolin activation and tears apart the continuous beta sheet core of G4 and G6.

Dynamic properties of actin. Structural changes induced by beryllium fluoride.

The BeFx-induced specific and distinct changes in G- and F-actin point to the dynamic nature of actin structure and the local differences between monomeric and polymeric forms of act in.

Atomic model of the actin filament

A unique orientation of the monomer with respect to the actin helix has been found and the main interactions are along the two-start helix with a contribution from a loop extending across the filament axis provided by the molecule in the adjacent strand.