4ZNO

Crystal structure of Dln1 complexed with sucrose

4ZNO の概要

• エントリーDOI: 10.2210/pdb4zno/pdb
• 関連するPDBエントリー: 4ZNQ 4ZNR
• 関連するBIRD辞書のPRD_ID: PRD_900003
• 分子名称: Natterin-like protein, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: pore-forming protein, aeolysin-like protein, vetebrate, high-mannose glycans, complex, sugar binding protein
• 由来する生物種: Danio rerio (Zebrafish)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73951.56

構造登録者

Jia, N.,Jiang, Y.L.,Cheng, W.,Wang, H.W.,Zhou, C.Z.,Chen, Y. (登録日: 2015-05-05, 公開日: 2016-01-20, 最終更新日: 2024-03-20)

主引用文献

Jia, N.,Liu, N.,Cheng, W.,Jiang, Y.L.,Sun, H.,Chen, L.L.,Peng, J.,Zhang, Y.,Ding, Y.H.,Zhang, Z.H.,Wang, X.,Cai, G.,Wang, J.,Dong, M.Q.,Zhang, Z.,Wu, H.,Wang, H.W.,Chen, Y.,Zhou, C.Z.
Structural basis for receptor recognition and pore formation of a zebrafish aerolysin-like protein.
Embo Rep., 17:235-248, 2016

PubMed Abstract: Various aerolysin-like pore-forming proteins have been identified from bacteria to vertebrates. However, the mechanism of receptor recognition and/or pore formation of the eukaryotic members remains unknown. Here, we present the first crystal and electron microscopy structures of a vertebrate aerolysin-like protein from Danio rerio, termed Dln1, before and after pore formation. Each subunit of Dln1 dimer comprises a β-prism lectin module followed by an aerolysin module. Specific binding of the lectin module toward high-mannose glycans triggers drastic conformational changes of the aerolysin module in a pH-dependent manner, ultimately resulting in the formation of a membrane-bound octameric pore. Structural analyses combined with computational simulations and biochemical assays suggest a pore-forming process with an activation mechanism distinct from the previously characterized bacterial members. Moreover, Dln1 and its homologs are ubiquitously distributed in bony fishes and lamprey, suggesting a novel fish-specific defense molecule.

PubMed: 26711430
DOI: 10.15252/embr.201540851

実験手法

X-RAY DIFFRACTION (1.86 Å)