ClpXP in Escherichia coli is a proteasome degrading protein substrates. It consists of one hexamer of ATPase (ClpX) and two heptamers of peptidase (ClpP). The ClpX binds ATP and translocates the substrate protein into the ClpP chamber by binding and hydrolysis of ATP. At single molecular level, ClpX harnesses cycles of power stroke (dwell and burst) to unfold the substrates, then releases the ADP and Pi. Based on the construction and function of ClpXP, especially the recent progress on how ClpX unfold protein substrates, in this mini-review, a currently proposed single ClpX molecular model system detected by optical tweezers, and its prospective for the elucidation of the mechanism of force generation of ClpX in its power stroke and the subunit interaction with each other, were discussed in detail.

大肠杆菌中的ClpXP是降解蛋白底物的蛋白酶体。它由一个ATPase的六聚体（ClpX）和两个肽酶的七聚体（ClpP）组成。ClpX结合ATP，并通过ATP的结合和水解将底物蛋白转移到ClpP室中。在单分子水平上，ClpX利用功率冲程循环（停顿和爆发）展开底物，然后释放ADP和Pi。基于ClpXP的结构和功能，特别是ClpX如何展开蛋白质底物的最新进展，在此迷你阅读中，当前提出的用光镊检测的单个ClpX分子模型系统及其对阐明力机制的展望详细讨论了ClpX在其动力冲程中的生成以及亚基之间的相互作用。