3J8K

Tilted state of actin, T2

Summary for 3J8K

• Entry DOI: 10.2210/pdb3j8k/pdb
• Related: 3J8I 3J8J
• EMDB information: 6179 6180 6181
• Descriptor: Actin, alpha skeletal muscle (1 entity in total)
• Functional Keywords: helical polymer, actin filament, structural protein
• Biological source: Oryctolagus cuniculus (rabbit)
• Total number of polymer chains: 10
• Total formula weight: 420969.53

Authors

Galkin, V.E.,Orlova, A.,Vos, M.R.,Schroder, G.F.,Egelman, E.H. (deposition date: 2014-11-07, release date: 2015-01-14, Last modification date: 2024-02-21)

Primary citation

Galkin, V.E.,Orlova, A.,Vos, M.R.,Schroder, G.F.,Egelman, E.H.
Near-atomic resolution for one state of f-actin.
Structure, 23:173-182, 2015

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 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.

PubMed: 25533486
DOI: 10.1016/j.str.2014.11.006

Experimental method

ELECTRON MICROSCOPY (12 Å)