RecA-like motor ATPases - lessons from structures

被引:117
作者
Ye, JQ
Osborne, AR
Groll, M
Rapoport, TA
机构
[1] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA
[2] Univ Munich, Inst Physiol Chem, D-81377 Munich, Germany
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2004年 / 1659卷 / 01期
基金
美国国家卫生研究院;
关键词
ATPase; RecA; structure; motor protein; oligomerization;
D O I
10.1016/j.bbabio.2004.06.003
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A large class of ATPases contains a RecA-like structural domain and uses the energy of nucleotide binding and hydrolysis to perform mechanical work, for example, to move polypeptides or nucleic acids. These ATPases include helicases, ABC transporters, clamp loaders, and proteases. The functional units of the ATPases contain different numbers of RecA-like domains, but the nucleotide is always bound at the interface between two adjacent RecA-like folds and the two domains move relative to one another during the ATPase cycle. The structures determined for different RecA-like motor ATPases begin to reveal how they move macromolecules. (C) 2004 Elsevier B.V. All rights reserved.
引用
收藏
页码:1 / 18
页数:18
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