Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, 405 Liverpool Street, Darlinghurst, NSW 2010, Australia.
Acta Crystallogr F Struct Biol Commun. 2021 Mar 1;77(Pt 3):79-84. doi: 10.1107/S2053230X21002223. Epub 2021 Mar 3.
Chaperonins are biomolecular complexes that assist in protein folding. Thermophilic factor 55 (TF55) is a group II chaperonin found in the archaeal genus Sulfolobus that has α, β and γ subunits. Using cryo-electron microscopy, structures of the β-only complex of S. solfataricus TF55 (TF55β) were determined to 3.6-4.2 Å resolution. The structures of the TF55β complexes formed in the presence of ADP or ATP highlighted an open state in which nucleotide exchange can occur before progressing in the refolding cycle.
伴侣蛋白是协助蛋白质折叠的生物分子复合物。嗜热因子 55（TF55）是一种在古菌属 Sulfolobus 中发现的 II 类伴侣蛋白，具有 α、β 和 γ 亚基。通过低温电子显微镜，确定了来自 S. solfataricus TF55（TF55β）的仅β复合物的结构，分辨率为 3.6-4.2 Å。在存在 ADP 或 ATP 的情况下形成的 TF55β 复合物的结构突出了一种开放状态，在这种状态下，核苷酸交换可以在折叠循环中进行之前发生。
