Grallert H, Buchner J
Institut für Organische Chemie und Biochemie, Technische Universität München, Garching, 85747, Germany.
J Struct Biol. 2001 Aug;135(2):95-103. doi: 10.1006/jsbi.2001.4387.
The GroE chaperone system consists of two ring-shaped oligomeric components whose association creates different functional states. The most remarkable property of the GroE system is the ability to fold proteins under conditions where spontaneous folding cannot occur. To achieve this, a fully functional system consisting of GroEL, the cochaperone GroES, and ATP is necessary. Driven by ATP binding and hydrolysis, this system cycles through different conformational stages, which allow binding, folding, and release of substrate proteins. Some aspects of the ATP-driven reaction cycle are still under debate. One of these open questions is the importance of so-called "football" complexes consisting of GroEL and two bound GroES rings. Here, we summarize the evidence for the functional relevance of these complexes and their involvement in the efficient folding of substrate proteins.
GroE伴侣系统由两个环状寡聚体组件组成，它们的结合会产生不同的功能状态。GroE系统最显著的特性是能够在无法自发折叠的条件下折叠蛋白质。要实现这一点，由GroEL、辅助伴侣GroES和ATP组成的全功能系统是必需的。在ATP结合和水解的驱动下，该系统循环经历不同的构象阶段，这些阶段允许底物蛋白的结合、折叠和释放。ATP驱动的反应循环的某些方面仍存在争议。这些未解决的问题之一是由GroEL和两个结合的GroES环组成的所谓“足球”复合物的重要性。在这里，我们总结了这些复合物功能相关性的证据及其在底物蛋白高效折叠中的作用。
