This title appears in the Scientific Report :
2011
Please use the identifier:
http://dx.doi.org/10.1073/pnas.1110109108 in citations.
Remodeling of actin filaments by ADF/cofilin proteins
Remodeling of actin filaments by ADF/cofilin proteins
Cofilin/ADF proteins play key roles in the dynamics of actin, one of the most abundant and highly conserved eukaryotic proteins. We used cryoelectron microscopy to generate a 9-Å resolution three-dimensional reconstruction of cofilin-decorated actin filaments, the highest resolution achieved for a c...
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Personal Name(s): | Galkin, V.E. |
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Orlova, A. / Kudryashov, D.S. / Solodukhin, A. / Reisler, E. / Schröder, G.F. / Egelman, E.H. | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | Proceedings of the National Academy of Sciences of the United States of America, 108 (2011) S. 20568 - 20572 |
Imprint: |
Washington, DC
Academy
2011
|
Physical Description: |
20568 - 20572 |
DOI: |
10.1073/pnas.1110109108 |
PubMed ID: |
22158895 |
Document Type: |
Journal Article |
Research Program: |
BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung Funktion und Dysfunktion des Nervensystems |
Series Title: |
Proceedings of the National Academy of Sciences of the United States of America
108 |
Subject (ZB): | |
Publikationsportal JuSER |
Cofilin/ADF proteins play key roles in the dynamics of actin, one of the most abundant and highly conserved eukaryotic proteins. We used cryoelectron microscopy to generate a 9-Å resolution three-dimensional reconstruction of cofilin-decorated actin filaments, the highest resolution achieved for a complex of F-actin with an actin-binding protein. We show that the cofilin-induced change in the filament twist is due to a unique conformation of the actin molecule unrelated to any previously observed state. The changes between the actin protomer in naked F-actin and in the actin-cofilin filament are greater than the conformational changes between G- and F-actin. Our results show the structural plasticity of actin, suggest that other actin-binding proteins may also induce large but different conformational changes, and show that F-actin cannot be described by a single molecular model. |