The crystal structure of uncomplexed actin in the ADP state
The crystal structure of uncomplexed actin in the ADP state
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DOI：
10.1126/science.1059700
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发表时间：
2001-07-27
期刊：
影响因子：
56.9
通讯作者：
Dominguez, R
中科院分区：
文献类型：
--
作者：
Otterbein, LR;Graceffa, P;Dominguez, R
肌动蛋白丝的动力学和极性由与腺苷S '-三磷酸（ATP）水解偶联的构象变化控制，其机制仍有待阐明。将修饰成嵌段聚合的肌动蛋白以腺苷5 '-二磷酸（ADP）状态结晶，并将结构解析至1.54埃分辨率。与以前的ATP-肌动蛋白的结构与脱氧核糖核酸酶I，profilin，凝胶蛋白复合物相比，单体ADP-肌动蛋白的特点是由一个显着的构象变化，在亚结构域2。单体肌动蛋白的成功结晶为将来肌动蛋白与肌动蛋白结合蛋白（如肌球蛋白）复合物的结构测定开辟了道路。
The dynamics and polarity of actin filaments are controlled by a conformational change coupled to the hydrolysis of adenosine S'-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 gelsotin, 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.