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000186656 1001_ $$0P:(DE-HGF)0$$aGalkin, Vitold E.$$b0
000186656 245__ $$aNear-Atomic Resolution for One State of F-Actin
000186656 260__ $$aLondon [u.a.]$$bElsevier Science$$c2015
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000186656 520__ $$aActin 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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000186656 7001_ $$0P:(DE-HGF)0$$aOrlova, Albina$$b1
000186656 7001_ $$0P:(DE-HGF)0$$aVos, Matthijn R.$$b2
000186656 7001_ $$0P:(DE-Juel1)132018$$aSchröder, Gunnar$$b3$$ufzj
000186656 7001_ $$0P:(DE-HGF)0$$aEgelman, Edward H.$$b4$$eCorresponding Author
000186656 773__ $$0PERI:(DE-600)2031189-8$$a10.1016/j.str.2014.11.006$$gVol. 23, no. 1, p. 173 - 182$$n1$$p173 - 182$$tStructure$$v23$$x0969-2126$$y2015
000186656 8564_ $$uhttp://www.sciencedirect.com/science/article/pii/S0969212614003724
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