4zno | pdb_00004zno

Crystal structure of Dln1 complexed with sucrose

spinqualitylabelsall models 4zno, resolution 1.86Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4zno is a 2 chain structure with sequence from Danio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, EPE, FRU, GLC, PRD_900003 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AEP1_DANRE Pore-forming protein which might play a role in host defense. Exists as an antiparallel dimer in solution. Can also assemble into an octameric pore-like structure spanning the cell membrane. Oligomerization may be triggered by binding of the jacalin-type lectin domain to high-mannose cell-surface proteoglycans, and also requires a low pH environment. In vitro, shows high binding affinity for S.cerevisiae mannan and human HIV virus glycoprotein gp120. Publication Abstract from PubMed 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 beta-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. Structural basis for receptor recognition and pore formation of a zebrafish aerolysin-like protein.,Jia N, Liu N, Cheng W, Jiang YL, Sun H, Chen LL, Peng J, Zhang Y, Ding YH, Zhang ZH, Wang X, Cai G, Wang J, Dong MQ, Zhang Z, Wu H, Wang HW, Chen Y, Zhou CZ EMBO Rep. 2015 Dec 28. pii: e201540851. PMID:26711430 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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