Close Identity between Alternatively Folded State N2 of Ubiquitin and the Conformation of the Protein Bound to the Ubiquitin-Activating Enzyme

详细信息    查看全文

• 作者：Soichiro Kitazawa ; Tomoshi Kameda ; Ayumi Kumo ; Maho Yagi-Utsumi ; Nicola J. Baxter ; Koichi Kato ; Mike P. Williamson ; Ryo Kitahara
• 刊名：Biochemistry
• 出版年：2014
• 出版时间：January 28, 2014
• 年：2014
• 卷：53
• 期：3
• 页码：447-449
• 全文大小：187K
• ISSN：1520-4995

文摘

We present the nuclear Overhauser effect-based structure determination of the Q41N variant of ubiquitin at 2500 bar, where the alternatively folded N₂ state is 97% populated. This allows us to characterize the structure of the 鈥減ure鈥?N₂ state of ubiquitin. The N₂ state shows a substantial change in the orientation of strand 尾₅ compared to that of the normal folded N₁ state, which matches the changes seen upon binding of ubiquitin to ubiquitin-activating enzyme E1. The recognition of E1 by ubiquitin is therefore best explained by conformational selection rather than induced-fit motion.