Otterbein L R, Graceffa P, Dominguez R
Boston Biomedical Research Institute, 64 Grove Street, Watertown, MA 02472, USA.
Science. 2001 Jul 27;293(5530):708-11. doi: 10.1126/science.1059700.
The dynamics and polarity of actin filaments are controlled by a conformational change coupled to the hydrolysis of adenosine 5'-triphosphate (ATP) by a mechanism that remains to be elucidated. Actin modified to block polymerization was crystallized in the adenosine 5'-diphosphate (ADP) state, and the structure was solved to 1.54 angstrom resolution. Compared with previous ATP-actin structures from complexes with deoxyribonuclease I, profilin, and gelsolin, monomeric ADP-actin is characterized by a marked conformational change in subdomain 2. The successful crystallization of monomeric actin opens the way to future structure determinations of actin complexes with actin-binding proteins such as myosin.
肌动蛋白丝的动力学和极性由一种与腺苷 5'-三磷酸（ATP）水解偶联的构象变化控制，其机制尚待阐明。经修饰以阻断聚合的肌动蛋白在腺苷 5'-二磷酸（ADP）状态下结晶，其结构解析至 1.54 埃分辨率。与先前来自与脱氧核糖核酸酶 I、肌动蛋白结合蛋白和凝溶胶蛋白复合物的 ATP -肌动蛋白结构相比，单体 ADP -肌动蛋白的特征是亚结构域 2 有显著的构象变化。单体肌动蛋白的成功结晶为未来测定肌动蛋白与肌球蛋白等肌动蛋白结合蛋白复合物的结构开辟了道路。
