2ZWH
Model for the F-actin structure
2ZWH の概要
| エントリーDOI | 10.2210/pdb2zwh/pdb |
| 分子名称 | Actin, alpha skeletal muscle, ADENOSINE-5'-DIPHOSPHATE, CALCIUM ION (3 entities in total) |
| 機能のキーワード | f-actin, g-actin, cytoskelton, contractile protein, atp-binding, cytoskeleton, methylation, muscle protein, nucleotide-binding, phosphoprotein |
| 由来する生物種 | Oryctolagus cuniculus (Rabbit) |
| 細胞内の位置 | Cytoplasm, cytoskeleton: P68135 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 42342.91 |
| 構造登録者 | Oda, T.,Iwasa, M.,Aihara, T.,Maeda, Y.,Narita, A. (登録日: 2008-12-05, 公開日: 2009-01-20, 最終更新日: 2025-03-26) |
| 主引用文献 | Oda, T.,Iwasa, M.,Aihara, T.,Maeda, Y.,Narita, A. The nature of the globular- to fibrous-actin transition. Nature, 457:441-445, 2009 Cited by 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: 19158791DOI: 10.1038/nature07685 主引用文献が同じPDBエントリー |
| 実験手法 | FIBER DIFFRACTION (3.3 Å) |
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