Atomic model of the actin filament

  title={Atomic model of the actin filament},
  author={Kenneth C. Holmes and David Popp and Werner Gebhard and Wolfgang Kabsch},
The F-actin filament has been constructed from the atomic structure of the actin monomer to fit the observed X-ray fibre diagram from oriented gels of F-actin. A unique orientation of the monomer with respect to the actin helix has been found. 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. There are also contacts along the left-handed genetic helix. 
The structure of the F-actin filament and the actin molecule.
Structure and Dynamics of F-actin: Conformational Change of Actin Molecule Induced by Polymerization
A novel flat conformation of actin molecule in F-actin structure is found using the X-ray fiber diffraction method and is deduced to be important for both the filament formation and the actin ATPase.
The crystal structure of a cross-linked actin dimer suggests a detailed molecular interface in F-actin.
A plausible model of F-actin can be constructed by reintroducing the known filament twist, without disturbing significantly the interface observed in the actin dimer crystal.
Structure and dynamics of the actin filament.
Molecular structure of F-actin and location of surface binding sites
Comparisons of three-dimensional maps of vertebrate muscle thin filaments obtained by cryo-electron microscopy and image analysis, reveal the molecular structure of F-actin, the location of the C
Vibrational modes of G-actin.
The structure of f-actin was deduced from x-ray diffraction patterns from bundles of aligned actin filaments, using the known helical symmetry of the filament and keeping the atomic structure of the monomer fixed, and the model was obtained using only four structural parameters.
An atomic model of crystalline actin tubes: combining electron microscopy with X-ray crystallography.
An integrated structural approach which combines intermediate resolution electron microscopy based 3-D reconstruction and surface metal shadowing of crystalline actin tubes with atomic resolution X-ray data of the G-actin monomer is chosen.
A comparison of the atomic model of F-actin with cryo-electron micrographs of actin and decorated actin.
The atomic model calculated from the crystal structure and the X-ray fiber diagram of orientated F-actin1) with the 3-D reconstructions produced from cryo-electron microscopy of actin2 are essentially identical.
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.


Molecular packing in profilin: actin crystals and its implications.
Structural relationships of actin, myosin, and tropomyosin revealed by cryo-electron microscopy
By comparing maps from decorated thin filaments with those from decorated actin, it is demonstrated that tropomyosin is bound to the inner domain of actin just in front of the myosin binding site at a radius of approximately 40 A.
The Three‐Dimensional Structure of the Actin Filament Revisited a
The recent observation by Trinick et a1.* that actin filaments exhibit variable crossovers even when embedded in a film of vitreous ice, without attachment to a substrate, supports the notion that this disorder is an intrinsic property of actin Filaments and not just a random variable twist.
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
Orientation of actin monomer in the F-actin filament: radial coordinate of glutamine-41 and effect of myosin subfragment 1 binding on the monomer orientation.
The method of radial distance measurements in order to orient the actin monomer in the F-actin filament found that if radial coordinates of four points are determined and six intramolecular distances are known, one can, within symmetry limits, position the monomer about the filament axis.
Role of nucleotide hydrolysis in the dynamics of actin filaments and microtubules.
  • M. Carlier
  • Biology
    International review of cytology
  • 1989
The nucleotide hydrolysis generates complex patterns of monomer concentration at steady state and during growth, which contrasts with the behavior of equilibrium polymers.
Movement of myosin-coated beads on oriented filaments reconstituted from purified actin
It is demonstrated for the first time that actin alone, linked to a substratum by a protein anchor, is sufficient to support movement of myosin at rates consistent with the speeds of muscle contraction and other forms of cell motility.