8HRU

Cryo-EM structure of ACE2

8HRU の概要

• エントリーDOI: 10.2210/pdb8hru/pdb
• EMDBエントリー: 34980
• 分子名称: Angiotensin-converting enzyme 2 (1 entity in total)
• 機能のキーワード: receptor of sars-cov-2, protein binding
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 72396.49

構造登録者

Xu, J.,Liu, N.,Wang, H.W. (登録日: 2022-12-16, 公開日: 2023-12-20, 最終更新日: 2025-01-01)

主引用文献

Zheng, L.,Xu, J.,Wang, W.,Gao, X.,Zhao, C.,Guo, W.,Sun, L.,Cheng, H.,Meng, F.,Chen, B.,Sun, W.,Jia, X.,Zhou, X.,Wu, K.,Liu, Z.,Ding, F.,Liu, N.,Wang, H.W.,Peng, H.
Self-assembled superstructure alleviates air-water interface effect in cryo-EM.
Nat Commun, 15:7300-7300, 2024

PubMed Abstract: Cryo-electron microscopy (cryo-EM) has been widely used to reveal the structures of proteins at atomic resolution. One key challenge is that almost all proteins are predominantly adsorbed to the air-water interface during standard cryo-EM specimen preparation. The interaction of proteins with air-water interface will significantly impede the success of reconstruction and achievable resolution. Here, we highlight the critical role of impenetrable surfactant monolayers in passivating the air-water interface problems, and develop a robust effective method for high-resolution cryo-EM analysis, by using the superstructure GSAMs which comprises surfactant self-assembled monolayers (SAMs) and graphene membrane. The GSAMs works well in enriching the orientations and improving particle utilization ratio of multiple proteins, facilitating the 3.3-Å resolution reconstruction of a 100-kDa protein complex (ACE2-RBD), which shows strong preferential orientation using traditional specimen preparation protocol. Additionally, we demonstrate that GSAMs enables the successful determinations of small proteins (<100 kDa) at near-atomic resolution. This study expands the understanding of SAMs and provides a key to better control the interaction of protein with air-water interface.

PubMed: 39181869
DOI: 10.1038/s41467-024-51696-w

実験手法

ELECTRON MICROSCOPY (3.9 Å)