The nature of the globular- to fibrous-actin transition Export

@article{citeulike:3922020, 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 \r{A} in the radial direction and 5.6 \r{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.}, author = {Oda, Toshiro and Iwasa, Mitsusada and Aihara, Tomoki and Maeda, Yuichiro and Narita, Akihiro}, citeulike-article-id = {3922020}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/nature07685}, citeulike-linkout-1 = {http://dx.doi.org/10.1038/nature07685}, day = {22}, doi = {10.1038/nature07685}, issn = {0028-0836}, journal = {Nature}, keywords = {actin}, month = {January}, number = {7228}, pages = {441--445}, posted-at = {2009-10-06 10:37:56}, priority = {2}, publisher = {Nature Publishing Group}, title = {The nature of the globular- to fibrous-actin transition}, url = {http://dx.doi.org/10.1038/nature07685}, volume = {457}, year = {2009} }

TY - JOUR ID - citeulike:3922020 L3 - citeulike-article-id:3922020 N2 - 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 Å in the radial direction and 5.6 Å 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. IS - 7228 JF - Nature SN - 0028-0836 EP - 445 TI - The nature of the globular- to fibrous-actin transition PB - Nature Publishing Group VL - 457 SP - 441 KW - actin AU - Oda, Toshiro AU - Iwasa, Mitsusada AU - Aihara, Tomoki AU - Maeda, Yuichiro AU - Narita, Akihiro PY - 2009/01/22/ UR - http://dx.doi.org/10.1038/nature07685 ER -