当前位置: X-MOL 学术Archaea › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Fundamental Characteristics of AAA+ Protein Family Structure and Function.
Archaea ( IF 2.3 ) Pub Date : 2016-09-14 , DOI: 10.1155/2016/9294307
Justin M Miller 1 , Eric J Enemark 1
Affiliation  

Many complex cellular events depend on multiprotein complexes known as molecular machines to efficiently couple the energy derived from adenosine triphosphate hydrolysis to the generation of mechanical force. Members of the AAA+ ATPase superfamily (ATPases Associated with various cellular Activities) are critical components of many molecular machines. AAA+ proteins are defined by conserved modules that precisely position the active site elements of two adjacent subunits to catalyze ATP hydrolysis. In many cases, AAA+ proteins form a ring structure that translocates a polymeric substrate through the central channel using specialized loops that project into the central channel. We discuss the major features of AAA+ protein structure and function with an emphasis on pivotal aspects elucidated with archaeal proteins.

中文翻译:

AAA +蛋白质家族结构和功能的基本特征。

许多复杂的细胞事件依赖于称为分子机器的多蛋白复合物,从而将三磷酸腺苷水解所产生的能量有效地耦合到机械力的产生上。AAA + ATPase超家族(与各种细胞活动相关的ATPase)的成员是许多分子机器的关键组成部分。AAA +蛋白由保守模块定义,该模块精确定位两个相邻亚基的活性位点元素以催化ATP水解。在许多情况下,AAA +蛋白形成一个环结构,该环结构使用伸入中央通道的专门环将聚合物底物通过中央通道移位。我们讨论了AAA +蛋白质结构和功能的主要特征,重点是古细菌蛋白质阐明的关键方面。
更新日期:2016-09-14
down
wechat
bug