5MVA
Structure of the thin filament at high calcium concentration
5MVA の概要
| エントリーDOI | 10.2210/pdb5mva/pdb |
| EMDBエントリー | 3576 |
| 分子名称 | Actin, alpha skeletal muscle, ADENOSINE-5'-DIPHOSPHATE (2 entities in total) |
| 機能のキーワード | thin filament, troponin, actin, tropomyosin, structural protein |
| 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 | 23 |
| 化学式量合計 | 972965.18 |
| 構造登録者 | |
| 主引用文献 | Paul, D.M.,Squire, J.M.,Morris, E.P. Relaxed and active thin filament structures; a new structural basis for the regulatory mechanism. J. Struct. Biol., 197:365-371, 2017 Cited by PubMed Abstract: The structures of muscle thin filaments reconstituted using skeletal actin and cardiac troponin and tropomyosin have been determined with and without bound Ca using electron microscopy and reference-free single particle analysis. The resulting density maps have been fitted with atomic models of actin, tropomyosin and troponin showing that: (i) the polarity of the troponin complex is consistent with our 2009 findings, with large shape changes in troponin between the two states; (ii) without Ca the tropomyosin pseudo-repeats all lie at almost equivalent positions in the 'blocked' position on actin (over subdomains 1 and 2); (iii) in the active state the tropomyosin pseudo-repeats are all displaced towards subdomains 3 and 4 of actin, but the extent of displacement varies within the regulatory unit depending upon the axial location of the pseudo-repeats with respect to troponin. Individual pseudo-repeats with Ca bound to troponin can be assigned either to the 'closed' state, a partly activated conformation, or the 'M-state', a fully activated conformation which has previously been thought to occur only when myosin heads bind. These results lead to a modified view of the steric blocking model of thin filament regulation in which cooperative activation is governed by troponin-mediated local interactions of the pseudo-repeats of tropomyosin with actin. PubMed: 28161413DOI: 10.1016/j.jsb.2017.01.004 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (27.7 Å) |
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