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Title | Near-atomic resolution for one state of F-actin. |
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Journal, issue, pages | Structure, Vol. 23, Issue 1, Page 173-182, Year 2015 |
Publish date | Jan 6, 2015 |
Authors | Vitold E Galkin / Albina Orlova / Matthijn R Vos / Gunnar F Schröder / Edward H Egelman / |
PubMed Abstract | 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 ...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. |
External links | Structure / PubMed:25533486 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 4.7 - 12.0 Å |
Structure data | |
Chemicals | ChemComp-ADP: ChemComp-MG: |
Source |
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Keywords | STRUCTURAL PROTEIN / helical polymer / F-actin / actin filament |