Atomic structure of the actin: DNase I complex

  title={Atomic structure of the actin: DNase I complex},
  author={Wolfgang Kabsch and Hans Georg Mannherz and Dietrich Suck and Emil F. Pai and Kenneth C. Holmes},
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 resolution of 2.8 Å and 3 Å, respectively. The two structures are very similar. The actin molecule consists of two domains which can be further subdivided into two subdomains. ADP or ATP is located in the cleft between the domains with a calcium ion bound to the β- or β- and γ-phosphates… 

The Crystal Structure of Uncomplexed Actin in the ADP State

The successful crystallization of monomeric actin opens the way to future structure determinations of actin complexes with actin-binding proteins such as myosin.

X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of Dictyostelium discoideum myosin to 2.7 A resolution.

BeFx complex with S1Dc suggests that the conformational change, which occurs when ATP binds to actomyosin and which reduces the affinity of myosin for actin, is caused by the binding of the gamma- and beta-phosphate groups of the nucleotide.

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.

The actin fold

  • W. KabschK. Holmes
  • Biology
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 1995
X‐ray structure analysis of actin and of the NH2‐terminal domain of the heat‐shock cognate protein Hsc70 has revealed an unexpected extensive structural similarity between these two molecules, suggesting that the molecules may have evolved by gene duplication.

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.

Evidence for an F-actin like conformation in the actin:DNase I complex.

It is demonstrated that a ribose modified analogue of ATP, TNP-ATP, can exchange with a resident nucleotide in F-actin, but fails to bind to G-actIn, consistent with the hypothesis that the two major domains of actin on either side of the cleft are able to "flex" or move relative to each other in G-acting, but that this flexing motion is limited as a consequence of either polymerisation or DNase I binding.

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.

The structure of an open state of beta-actin at 2.65 A resolution.

Applying osmotic pressure to profilin:beta-actin crystals brings about a collapse of the unit cell comparable with that seen in the open to tight-state transition, enabling an estimate of the work required to cause this transformation of beta- actin in the crystals.

X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-.

The three-dimensional structures of the truncated myosin head from Dictyostelium discoideum myOSin II complexed with beryllium and aluminum fluoride and magnesium ADP are reported, indicating that myos in undergoes a conformational change during hydrolysis that is not associated with the nucleotide binding pocket but rather occurs in the COOH-terminal segment of the myosIn motor domain.



Three-dimensional structure of the complex of skeletal muscle actin and bovine pancreatic DNAse I at 6-A resolution.

The structure of rabbit skeletal muscle actin complexed with bovine pancreatic DNase I has been determined by x-ray crystallographic methods at 6-A resolution. The analysis was based on a new

Three‐dimensional structure of the complex of actin and DNase I at 4.5 A resolution.

The shape of an actin subunit has been derived from an improved 6 A map of the complex of rabbit skeletal muscle actin and bovine pancreatic DNase I obtained by X‐ray crystallographic methods and the correct hand of the actin structure is determined from theDNase I atomic structure.

Proteolysis and structure of skeletal muscle actin.

  • D. MornetK. Ue
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1984
Under standard conditions, G-actin has been submitted to nine proteases of varying specificity, and in each case the pattern of fragments produced has been studied by NaDodSO4 gel electrophoresis, suggesting that the actin monomer consists of a large region and a small, easily degraded region.

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

Surprisingly, the nucleotide-binding 'core' of the ATPase fragment has a tertiary structure similar to that of hexokinase, although the remainder of the structures of the two proteins are completely dissimilar, suggesting that both the phosphotransferase mechanism and the substrate-induced conformational change intrinsic to the hexokinases may be used by the 70K heat shock-related proteins.

Structure refined to 2Å of a nicked DNA octanucleotide complex with DNase I

The cutting rates of bovine pancreatic deoxyribonuclease I (DNase I) vary along a given DNA sequence, indicating that the enzyme recognizes sequence-dependent structural variations of the DNA

Three‐dimensional structure of bovine pancreatic DNase I at 2.5 A resolution.

The three‐dimensional structure of bovine pancreatic deoxyribonuclease I (DNase I) has been determined at 2.5 A resolution by X‐ray diffraction from single crystals and the electron density map indicates that two Ca2+ ions are bound to the enzyme under crystallization conditions.

Crystallization and preliminary crystallographic data of chicken gizzard G-actin . DNase I complex and Physarum G-actin . DNase I complex.

Smooth muscle G-actin from chicken gizzard and Physarum plasmodium G-actsin both interact with DNase I and form 1 : 1 complexes, which belong to the same orthorhombic space group P2(1)2( 1)2 (1) 2(1).