Reference: Egelman EH and Orlova A (2001) Two conformations of G-actin related to two conformations of F-actin. Results Probl Cell Differ 32:95-101

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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.

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Journal Article | Research Support, U.S. Gov't, P.H.S. | Review
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Egelman EH, Orlova A
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