Ye Jiqing, Osborne Andrew R, Groll Michael, Rapoport Tom A
Department of Cell Biology, Harvard Medical School, HHMI, 240 Longwood Ave., LHRRB 613, Boston, MA 02115, USA.
Biochim Biophys Acta. 2004 Nov 4;1659(1):1-18. doi: 10.1016/j.bbabio.2004.06.003.
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.
一大类ATP酶含有一个类RecA结构域,并利用核苷酸结合和水解的能量来执行机械工作,例如移动多肽或核酸。这些ATP酶包括解旋酶、ABC转运蛋白、钳位装载器和蛋白酶。ATP酶的功能单元包含不同数量的类RecA结构域,但核苷酸总是结合在两个相邻类RecA折叠之间的界面处,并且在ATP酶循环过程中两个结构域相对彼此移动。针对不同类RecA运动ATP酶确定的结构开始揭示它们如何移动大分子。