This title appears in the Scientific Report :
2015
Please use the identifier:
http://dx.doi.org/10.1016/j.str.2014.11.006 in citations.
Near-Atomic Resolution for One State of F-Actin
Near-Atomic Resolution for One State of F-Actin
Actin functions as a helical polymer, F-actin, but attempts to build an atomic model for this filament have been hampered by the fact that the filament cannot be crystallized and by structural heterogeneity. We have used a direct electron detector, cryo-electron microscopy, and the forces imposed on...
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Personal Name(s): | Galkin, Vitold E. |
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Orlova, Albina / Vos, Matthijn R. / Schröder, Gunnar / Egelman, Edward H. (Corresponding Author) | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | Structure, 23 (2015) 1, S. 173 - 182 |
Imprint: |
London [u.a.]
Elsevier Science
2015
|
DOI: |
10.1016/j.str.2014.11.006 |
PubMed ID: |
25533486 |
Document Type: |
Journal Article |
Research Program: |
Functional Macromolecules and Complexes |
Publikationsportal JuSER |
Actin functions as a helical polymer, F-actin, but attempts to build an atomic model for this filament have been hampered by the fact that the filament cannot be crystallized and by structural heterogeneity. We have used a direct electron detector, cryo-electron microscopy, and the forces imposed on actin filaments in thin films to reconstruct one state of the filament at 4.7 Å resolution, which allows for building a reliable pseudo-atomic model of F-actin. We also report a different state of the filament where actin protomers adopt a conformation observed in the crystal structure of the G-actin-profilin complex with an open ATP-binding cleft. Comparison of the two structural states provides insights into ATP-hydrolysis and filament dynamics. The atomic model provides a framework for understanding why every buried residue in actin has been under intense selective pressure. |