3j8i | pdb_00003j8i

Near-Atomic Resolution for One State of F-Actin

spinqualitylabelsall models 3j8i, resolution 4.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3j8i is a 5 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, MG Related: 3j8j, 3j8k Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Publication Abstract from PubMed 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 A 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. Near-atomic resolution for one state of f-actin.,Galkin VE, Orlova A, Vos MR, Schroder GF, Egelman EH Structure. 2015 Jan 6;23(1):173-82. doi: 10.1016/j.str.2014.11.006. Epub 2014 Dec, 18. PMID:25533486 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Actin

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