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

Results Probl Cell Differ. 2001:32:95-101. doi: 10.1007/978-3-540-46560-7_7.

Abstract

In summary, a number of different conformational states of F-actin have been described by several different laboratories. Crystal structures have revealed that an opening of the nucleotide-binding cleft, produced by a large rotation of subdomain 2, can occur in G-actin. We have 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. This suggests that some of the dynamics associated with G-actin may provide insights into dynamic processes within the F-actin filament.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Actins / chemistry*
  • Actins / genetics
  • Mutation
  • Protein Conformation
  • Yeasts / chemistry*
  • Yeasts / genetics

Substances

  • Actins