8HYN

Bacterial STING from Riemerella anatipestifer

8HYN の概要

• エントリーDOI: 10.2210/pdb8hyn/pdb
• 分子名称: CD-NTase-associated protein 12, TETRAETHYLENE GLYCOL (3 entities in total)
• 機能のキーワード: cd-ntase-associated protein 12, signaling protein
• 由来する生物種: Riemerella anatipestifer Yb2
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37516.34

構造登録者

Wang, Y.-C.,Yang, C.-S.,Hou, M.-H.,Chen, Y. (登録日: 2023-01-07, 公開日: 2024-01-10, 最終更新日: 2024-01-24)

主引用文献

Hou, M.H.,Wang, Y.C.,Yang, C.S.,Liao, K.F.,Chang, J.W.,Shih, O.,Yeh, Y.Q.,Sriramoju, M.K.,Weng, T.W.,Jeng, U.S.,Hsu, S.D.,Chen, Y.
Structural insights into the regulation, ligand recognition, and oligomerization of bacterial STING.
Nat Commun, 14:8519-8519, 2023

PubMed Abstract: The cyclic GMP-AMP synthase (cGAS)/stimulator of interferon gene (STING) signaling pathway plays a critical protective role against viral infections. Metazoan STING undergoes multilayers of regulation to ensure specific signal transduction. However, the mechanisms underlying the regulation of bacterial STING remain unclear. In this study, we determined the crystal structure of anti-parallel dimeric form of bacterial STING, which keeps itself in an inactive state by preventing cyclic dinucleotides access. Conformational transition between inactive and active states of bacterial STINGs provides an on-off switch for downstream signaling. Some bacterial STINGs living in extreme environment contain an insertion sequence, which we show codes for an additional long lid that covers the ligand-binding pocket. This lid helps regulate anti-phage activities. Furthermore, bacterial STING can bind cyclic di-AMP in a triangle-shaped conformation via a more compact ligand-binding pocket, forming spiral-shaped protofibrils and higher-order fibril filaments. Based on the differences between cyclic-dinucleotide recognition, oligomerization, and downstream activation of different bacterial STINGs, we proposed a model to explain structure-function evolution of bacterial STINGs.

PubMed: 38129386
DOI: 10.1038/s41467-023-44052-x

実験手法

X-RAY DIFFRACTION (2.089 Å)