泛素连接酶
泛素
铰链
机制(生物学)
化学
生物物理学
分子动力学
泛素蛋白连接酶类
领域(数学分析)
细胞生物学
生物
物理
生物化学
基因
数学分析
计算化学
数学
经典力学
量子力学
作者
Kazusa Takeda,Holger Flechsig,Ikumi Muro,Romain Amyot,Fuminori Kobayashi,Noriyuki Kodera,Toshio Ando,Hiroki Konno
出处
期刊:Nano Letters
[American Chemical Society]
日期:2023-12-06
卷期号:23 (24): 11940-11948
被引量:3
标识
DOI:10.1021/acs.nanolett.3c04150
摘要
Ubiquitin (Ub) ligases E3 are important factors in selecting target proteins for ubiquitination and determining the type of polyubiquitin chains on the target proteins. In the HECT (homologous to E6AP C-terminus)-type E3 ligases, the HECT domain is composed of an N-lobe and a C-lobe that are connected by a flexible hinge loop. The large conformational rearrangement of the HECT domain via the flexible hinge loop is essential for the HECT-type E3-mediated Ub transfer from E2 to a target protein. However, detailed insights into the structural dynamics of the HECT domain remain unclear. Here, we provide the first direct demonstration of the structural dynamics of the HECT domain using high-speed atomic force microscopy at the nanoscale. We also found that the flexibility of the hinge loop has a great impact not only on its structural dynamics but also on the formation mechanism of free Ub chains.
科研通智能强力驱动
Strongly Powered by AbleSci AI