Two conformations of G-actin related to two conformations of F-actin.
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.
Egelman
E H
EH
Department of Biochemistry & Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908-0733, USA.
Orlova
A
A
D000199:Actins / Q000737:chemistry* / Q000235:genetics; D009154:Mutation; D011487:Protein Conformation; D015003:Yeasts / Q000737:chemistry* / Q000235:genetics
D000199:Actins