Near-Atomic Resolution for One State of F-Actin

Galkin, Vitold E.; Schröder, Gunnar; Orlova, Albina; Egelman, Edward H.; Vos, Matthijn R.

doi:10.1016/j.str.2014.11.006

Journal Article

FZJ-2015-00729

Near-Atomic Resolution for One State of F-Actin

Galkin, V. ; Orlova, A. ; Vos, M. ; Schröder, G.FZJ* ; Egelman, E. (Corresponding Author)

2015
Elsevier Science London [u.a.]

Structure 23(1), 173 - 182 (2015) [10.1016/j.str.2014.11.006]

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Please use a persistent id in citations: doi:10.1016/j.str.2014.11.006

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 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.

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