PDBsum entry 4zno

Sugar binding protein

PDB id: 4zno

Contents

Protein chains

318 a.a.

Ligands

GLC-FRU ×2

EPE

Metals

_CL ×2

Waters ×666

PDB id:

4zno

Name:

Sugar binding protein

Title:

Crystal structure of dln1 complexed with sucrose

Structure:

Natterin-like protein. Chain: a, b. Engineered: yes

Source:

Danio rerio. Zebrafish. Organism_taxid: 7955. Gene: zgc:113413. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.86Å R-factor: 0.191 R-free: 0.225

Authors:

N.Jia,Y.L.Jiang,W.Cheng,H.W.Wang,C.Z.Zhou,Y.Chen

Key ref:

N.Jia et al. (2016). Structural basis for receptor recognition and pore formation of a zebrafish aerolysin-like protein. Embo Rep, 17, 235-248. PubMed id: 26711430 DOI: 10.15252/embr.201540851

Date:

05-May-15 Release date: 20-Jan-16

Protein chains

Q5CZR5  (AEP1_DANRE) -  Aerolysin-like protein from Danio rerio

Seq: 315 a.a.

Struc: 318 a.a.

DOI no: 10.15252/embr.201540851

Embo Rep 17:235-248 (2016)

PubMed id: 26711430

Structural basis for receptor recognition and pore formation of a zebrafish aerolysin-like protein.

N.Jia, N.Liu, W.Cheng, Y.L.Jiang, H.Sun, L.L.Chen, J.Peng, Y.Zhang, Y.H.Ding, Z.H.Zhang, X.Wang, G.Cai, J.Wang, M.Q.Dong, Z.Zhang, H.Wu, H.W.Wang, Y.Chen, C.Z.Zhou.

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.