The crystal structure of uncomplexed actin in the ADP state

被引：417

作者：

Otterbein, LR ^{[1
]}

Graceffa, P ^{[1
]}

Dominguez, R ^{[1
]}

机构：

[1] Boston Biomed Res Inst, Watertown, MA 02472 USA

来源：

SCIENCE | 2001年 / 293卷 / 5530期

关键词：

D O I：

10.1126/science.1059700

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：708 / 711

页数：4

共 28 条

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