2ZWH

Model for the F-actin structure

Summary for 2ZWH

• Entry DOI: 10.2210/pdb2zwh/pdb
• Descriptor: Actin, alpha skeletal muscle, ADENOSINE-5'-DIPHOSPHATE, CALCIUM ION (3 entities in total)
• Functional Keywords: f-actin, g-actin, cytoskelton, contractile protein, atp-binding, cytoskeleton, methylation, muscle protein, nucleotide-binding, phosphoprotein
• Biological source: Oryctolagus cuniculus (Rabbit)
• Cellular location: Cytoplasm, cytoskeleton: P68135
• Total number of polymer chains: 1
• Total formula weight: 42342.91

Authors

Oda, T.,Iwasa, M.,Aihara, T.,Maeda, Y.,Narita, A. (deposition date: 2008-12-05, release date: 2009-01-20, Last modification date: 2025-03-26)

Primary citation

Oda, T.,Iwasa, M.,Aihara, T.,Maeda, Y.,Narita, A.
The nature of the globular- to fibrous-actin transition.
Nature, 457:441-445, 2009

PubMed Abstract: 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.

PubMed: 19158791
DOI: 10.1038/nature07685

Experimental method

FIBER DIFFRACTION (3.3 Å)