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Structure paper

TitleStructural basis for receptor recognition and pore formation of a zebrafish aerolysin-like protein.
Journal, issue, pagesEMBO Rep, Vol. 17, Issue 2, Page 235-248, Year 2016
Publish dateDec 28, 2015
AuthorsNing Jia / Nan Liu / Wang Cheng / Yong-Liang Jiang / Hui Sun / Lan-Lan Chen / Junhui Peng / Yonghui Zhang / Yue-He Ding / Zhi-Hui Zhang / Xuejuan Wang / Gang Cai / Junfeng Wang / Meng-Qiu Dong / Zhiyong Zhang / Hui Wu / Hong-Wei Wang / Yuxing Chen / Cong-Zhao Zhou /
PubMed AbstractVarious 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 ...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.
External linksEMBO Rep / PubMed:26711430 / PubMed Central
MethodsEM (electron crystallography) / X-ray diffraction
Resolution1.7 - 20.0 Å
Structure data

EMDB-3244:
Electron negative-staining microscopy of an aerolysin-like protein
Method: EM (electron crystallography) / Resolution: 20.0 Å

PDB-4zno:
Crystal structure of Dln1 complexed with sucrose
Method: X-RAY DIFFRACTION / Resolution: 1.86 Å

PDB-4znq:
Crystal structure of Dln1 complexed with Man(alpha1-2)Man
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-4znr:
Crystal structure of Dln1 complexed with Man(alpha1-3)Man
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-5di0:
Crystal structure of Dln1
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

Source
  • danio rerio (zebrafish)
KeywordsSUGAR BINDING PROTEIN / Pore-forming protein / Aeolysin-like protein / Vetebrate / High-mannose glycans / Complex

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