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Hemolytic Lectin CEL-III Heptamerizes via a Large Structural Transition from α-Helices to a β-Barrel during the Transmembrane Pore Formation Process


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Title: Hemolytic Lectin CEL-III Heptamerizes via a Large Structural Transition from α-Helices to a β-Barrel during the Transmembrane Pore Formation Process
Authors: Unno, Hideaki / Goda, Shuichiro / Hatakeyama, Tomomitsu
Issue Date: 2-May-2014
Publisher: American Society for Biochemistry and Molecular Biology Inc.
Citation: Journal of Biological Chemistry, 289(18), pp.12805-12812; 2014
Abstract: CEL-III is a hemolytic lectin isolated from the sea cucumber Cucumaria echinata. This lectin is composed of two carbohydrate-binding domains (domains 1 and 2) and one oligomerization domain (domain 3). After binding to the cell surface carbohydrate chains through domains 1 and 2, domain 3 self-associates to form transmembrane pores, leading to cell lysis or death, which resembles other pore-forming toxins of diverse organisms. To elucidate the pore formation mechanism of CEL-III, the crystal structure of the CEL-III oligomer was determined. The CEL-III oligomer has a heptameric structure with a long β-barrel as a transmembrane pore. This β-barrel is composed of 14 β-strands resulting from a large structural transition of α-helices accommodated in the interface between domains 1 and 2 and domain 3 in the monomeric structure, suggesting that the dissociation of these α-helices triggered their structural transition into a β-barrel. After heptamerization, domains 1 and 2 form a flat ring, in which all carbohydrate-binding sites remain bound to cell surface carbohydrate chains, stabilizing the transmembrane β-barrel in a position perpendicular to the plane of the lipid bilayer.
Keywords: carbohydrate / lectin / membrane / toxins / X-ray crystallography / β-barrel / hemolysin / oligomer / pore-forming toxin
URI: http://hdl.handle.net/10069/34459
ISSN: 00219258
DOI: 10.1074/jbc.M113.541896
Rights: This research was originally published in Journal of Biological Chemistry. Unno, H. et al. Hemolytic lectin cel-iii heptamerizes via a large structural transition from α-helices to a β-barrel during the transmembrane pore formation process. Journal of Biological Chemistry. 2014; Vol:289(18) pp.12805-12812. © the American Society for Biochemistry and Molecular Biology.
Type: Journal Article
Text Version: author
Appears in Collections:Articles in academic journal

Citable URI : http://hdl.handle.net/10069/34459

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