2zwh | pdb_00002zwh

Model for the F-actin structure

spinqualitylabelsall models 2zwh, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zwh is a 1 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, CA NonStd Res: HIC Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Actin plays crucial parts in cell motility through a dynamic process driven by polymerization and depolymerization, that is, the globular (G) to fibrous (F) actin transition. Although our knowledge about the actin-based cellular functions and the molecules that regulate the G- to F-actin transition is growing, the structural aspects of the transition remain enigmatic. We created a model of F-actin using X-ray fibre diffraction intensities obtained from well oriented sols of rabbit skeletal muscle F-actin to 3.3 A in the radial direction and 5.6 A along the equator. Here we show that the G- to F-actin conformational transition is a simple relative rotation of the two major domains by about 20 degrees. As a result of the domain rotation, the actin molecule in the filament is flat. The flat form is essential for the formation of stable, helical F-actin. Our F-actin structure model provides the basis for understanding actin polymerization as well as its molecular interactions with actin-binding proteins. The nature of the globular- to fibrous-actin transition.,Oda T, Iwasa M, Aihara T, Maeda Y, Narita A Nature. 2009 Jan 22;457(7228):441-5. PMID:19158791 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Actin F-actin

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