Identification of an allosteric network that influences assembly and function of group II chaperonins

Nature Structural & Molecular Biology, Published online: 7 September 2017; doi:10.1038/nsmb.3459

Group II chaperonins facilitate protein folding by undergoing ATP-driven conformational changes. A recent study reveals a tunable allosteric network in group II chaperonins that includes a residue at the intersubunit interface, which is important for assembly and allosteric coordination. The authors also propose that lower cooperativity allows group II chaperonins to achieve optimal substrate folding over a broad range of ATP concentrations.

中文翻译：

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识别影响II类伴侣蛋白装配和功能的变构网络

识别影响II类伴侣蛋白装配和功能的变构网络

《自然结构与分子生物学》，在线发布：2017年9月7日；doi：10.1038 / nsmb.3459

II组伴侣蛋白通过进行ATP驱动的构象变化来促进蛋白质折叠。最近的一项研究揭示了II组伴侣蛋白中的可调变构网络，该变构网络在亚基间界面处包含一个残基，这对于组装和变构协调非常重要。作者还提出，较低的协同性使II组分子伴侣在较宽的ATP浓度范围内实现最佳的底物折叠。