%0 Journal Article
%A Galkin, Vitold E.
%A Orlova, Albina
%A Vos, Matthijn R.
%A Schröder, Gunnar
%A Egelman, Edward H.
%T Near-Atomic Resolution for One State of F-Actin
%J Structure
%V 23
%N 1
%@ 0969-2126
%C London [u.a.]
%I Elsevier Science
%M FZJ-2015-00729
%P 173 - 182
%D 2015
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000347469500021
%$ pmid:25533486
%R 10.1016/j.str.2014.11.006
%U https://juser.fz-juelich.de/record/186656