The structure of crystalline profilin–β-actin

  title={The structure of crystalline profilin–$\beta$-actin},
  author={Clarence Schutt and James C. Myslik and Michael D. Rozycki and Nalin C. W. Goonesekere and Uno Lindberg},
The three-dimensional structure of bovine profilin–β-actin has been solved to 2.55 Å resolution by X-ray crystallography. There are several significant local changes in the structure of β-actin compared with α-actin as well as an overall 5° rotation between its two major domains. Actin molecules in the crystal are organized into ribbons through intermolecular contacts like those found in oligomeric protein assemblies. Profilin forms two extensive contacts with the actin ribbon, one of which… 

Structural aspects of actin-binding proteins.

Structural studies on the ribbon-to-helix transition in profilin: actin crystals.

A preliminary comparison of two states of profilin:beta-actin crystals shows that crystal polymorphism involves movements of actin subdomains at hinge points homologous to those found in hexokinase, a protein whose polypeptide fold is related to actin.

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.

Actin-Binding Protein Complexes at Atomic Resolution

This review describes three structures of actin complexed with different monomer-binding proteins, namely with DNase I, gelsolin segment 1, and profilin, which reflect the underlying structural fold of each.

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

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

Two conformations of G-actin related to two conformations of F-actin.

It is shown that two crystal states of beta-actin, in an open and closed form, can provide a very good model for the conformational difference in F-Actin between yeast the wild-type and a V159N mutant.

Crystallization and preliminary X-ray analysis of human platelet profilin complexed with an oligo proline peptide.

  • N. MahoneyS. Almo
  • Chemistry
    Acta crystallographica. Section D, Biological crystallography
  • 1998
The crystallization of the complex between human platelet profilin (HPP) and an L-proline decamer [(Pro)10] is reported here and Diffraction from these crystals is consistent with the space group P21212 with unit-cell constants.

Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation

The 2.2 Å X-ray structure of the complex between human platelet profilin (HPP) and a decamer of L-proline (L-Pro10) suggests a mechanism for the localization of prof ilin and its actin-related activities to sites of actin filament assembly in vivo.

Crystal packing induces a conformational change in profilin-I from Acanthamoeba castellanii.

This work used the second crystal structure as a test molecule in the molecular replacement procedure to determine the structure of the first crystal form of profilin-I, a 13-kDa protein that binds actin and poly-l-proline from Acanthamoeba castellanii.

F-actin-binding proteins.

  • A. McGough
  • Chemistry, Biology
    Current opinion in structural biology
  • 1998



Molecular packing in profilin: actin crystals and its implications.

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

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.

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

The structure of the E. coli recA protein monomer and polymer

The crystal structure of the recA protein from Escherichia coli at 2.3-Å resolution reveals a major domain that binds ADP and probably single- and double-stranded DNA. Two smaller subdomains at the N

Mechanism of the interaction of human platelet profilin with actin

It is suggested that the in vitro effects on actin polymerization may be explained by a complex mechanism that includes weak capping of filament ends and catalytic poisoning of nucleation, and although platelets contain only 1profilin for every 5-10 actin molecules, these complex reactions may allow substoichiometric profilin to have an important influence on act in assembly.

Normal mode analysis of G-actin.

A normal mode analysis of the G-actin monomer bound with ADP and Ca2+, in order to better understand the internal modes of this protein shows that the softest modes are almost identical.