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5DI0

Crystal structure of Dln1

Summary for 5DI0
Entry DOI10.2210/pdb5di0/pdb
Related4ZNO
DescriptorNatterin-like protein, 1,2-ETHANEDIOL, DI(HYDROXYETHYL)ETHER, ... (7 entities in total)
Functional Keywordspore-forming protein, aeolysin-like protein, vetebrate, high-mannose glycans, complex, sugar binding protein
Biological sourceDanio rerio (Zebrafish)
Total number of polymer chains2
Total formula weight76839.01
Authors
Jia, N.,Jiang, Y.L.,Cheng, W.,Wang, H.W.,Zhou, C.Z.,Chen, Y. (deposition date: 2015-08-31, release date: 2016-02-03, Last modification date: 2023-11-08)
Primary citationJia, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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