Staphylococcus aureus hibernation promoting factor (SaHPF) is a 22,2 kDa protein which plays a crucial role in 100S Staphylococcus aureus ribosome formation during stress. SaHPF consists of N-terminal domain (NTD) that prevents proteins synthesis by binding to the 30S subunit at the P- and A-sites, connected through a flexible linker with a C-terminal domain (CTD) that keeps ribosomes in 100S form via homodimerization. Recently obtained 100S ribosome structure of S. aureus by cryo-EM shown that SaHPF-NTD bound to the ribosome active sites, however due to the absence of SaHPF-NTD structure it was modeled by homology with the E. coli hibernation factors HPF and YfiA. In present paper we have determined the solution structure of SaHPF-NTD by high-resolution NMR spectroscopy which allows us to increase structural knowledge about HPF structure from S. aureus.

中文翻译：

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金黄色葡萄球菌冬眠促进因子N端结构域的溶液结构。

金黄色葡萄球菌冬眠促进因子 (SaHPF) 是一种 22,2 kDa 的蛋白质，在应激过程中在 100S 金黄色葡萄球菌核糖体形成中起关键作用。SaHPF 由 N 端结构域 (NTD) 组成，它通过与 P 和 A 位点的 30S 亚基结合来阻止蛋白质合成，通过一个灵活的接头与 C 端结构域 (CTD) 连接，使核糖体保持 100S 形式同二聚化。最近通过冷冻电镜获得的金黄色葡萄球菌的 100S 核糖体结构表明，SaHPF-NTD 与核糖体活性位点结合，但是由于不存在 SaHPF-NTD 结构，它通过与大肠杆菌休眠因子 HPF 和 YfiA 的同源性建模. 在本文中，我们通过高分辨率 NMR 光谱确定了 SaHPF-NTD 的溶液结构，这使我们能够从 S 中增加关于 HPF 结构的结构知识。