Fundamental Characteristics of AAA+ Protein Family Structure and Function

IF 2.3 4区 生物学 Q3 MICROBIOLOGY
Justin M. Miller, E. J. Enemark
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引用次数: 75

Abstract

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.
AAA+蛋白家族结构与功能的基本特征
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,以有效地将三磷酸腺苷水解产生的能量偶联到机械力的产生。AAA+ atp酶超家族成员(与各种细胞活动相关的atp酶)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件以催化ATP水解。在许多情况下,AAA+蛋白形成一个环形结构,利用投射到中心通道的特殊环将聚合底物通过中心通道进行易位。我们讨论了AAA+蛋白的结构和功能的主要特点,重点阐述了古细菌蛋白的关键方面。
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来源期刊
CiteScore
7.50
自引率
0.00%
发文量
1
审稿时长
>12 weeks
期刊介绍: Archaea is a peer-reviewed, Open Access journal that publishes original research articles as well as review articles dealing with all aspects of archaea, including environmental adaptation, enzymology, genetics and genomics, metabolism, molecular biology, molecular ecology, phylogeny, and ultrastructure. Bioinformatics studies and biotechnological implications of archaea will be considered. Published since 2002, Archaea provides a unique venue for exchanging information about these extraordinary prokaryotes.
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