期刊
JOURNAL OF STRUCTURAL BIOLOGY
卷 148, 期 3, 页码 259-267出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2004.07.003
关键词
RecA fold; AAA; mechanical properties; forces; ring structures
The oligomeric rings formed by RecA-fold proteins are mechanochemical motors that perform many important biological functions. Their RecA-fold domains convert the chemical energy of ATP into mechanical work through large nucleotide-dependent conformational changes. This review summarizes recent structural and mechanistic works on the F1-ATPase and HslU regarding to the force generation by individual RecA folds in the context of ring structures. The F1-ATPase ring for example generates the force perpendicular to the ring axis, while the HslU ring generates forces presumably parallel to it. There exists a strong correlation between the directions of forces generated and the orientation of the RecA folds, not only in these two proteins but also in T7 DNA helicase, suggesting that it should be possible to predict the direction of forces generated by other members of this family on the basis of the orientation of their RecA folds. (C) 2004 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据