Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata : Implications of domain structure for its membrane pore-formation mechanism

Uchida, Tatsuya; Yamasaki, Takayuki; Eto, Seiichiro; Sugawara, Hajime; Kurisu, Genji; Nakagawa, Atushi; Kusunoki, Masami; Hatakeyama, Tomomitsu

doi:info:doi/10.1074/jbc.M404065200

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タイトル	Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata : Implications of domain structure for its membrane pore-formation mechanism
著者	Uchida, Tatsuya Uchida, Tatsuya
	Yamasaki, Takayuki Yamasaki, Takayuki
	Eto, Seiichiro Eto, Seiichiro
	Sugawara, Hajime Sugawara, Hajime
	Kurisu, Genji Kurisu, Genji
	Nakagawa, Atushi Nakagawa, Atushi
	Kusunoki, Masami Kusunoki, Masami
	Hatakeyama, Tomomitsu Hatakeyama, Tomomitsu
内容	This research was originally published in Journal of Biological Chemistry. Tatsuya Uchida, Takayuki Yamasaki, Seiichiro Eto, Hajime Sugawara, Genji Kurisu, Atsushi Nakagawa, Masami Kusunoki and Tomomitsu Hatakeyama. Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata : Implications of domain structure for its membrane pore-formation mechanism. Journal of Biological Chemistry. 2004; 279, 37133-37141. © the American Society for Biochemistry and Molecular Biology.
抄録	CEL-III is a Ca^<2＋>＋ -dependent and galactose-specific lectin purified from the sea cucumber, Cucumaria echinata, which exhibits hemolytic and hemagglutinating activities. Six molecules of CEL-III are assumed to oligomerize to form an ion-permeable pore in the cell membrane. We have determined the crystal structure of CEL-III by using single isomorphous replacement aided by anomalous scattering in lead at 1.7 Å resolution. CEL-III consists of three distinct domains as follows: the N-terminal two carbohydrate-binding domains (1 and 2), which adopt β-trefoil folds such as the B-chain of ricin and are members of the (QXW)_3 motif family; and domain 3, which is a novel fold composed of two α-helices and one β-sandwich. CEL-III is the first Ca^<2＋> -dependent lectin structure with two β-trefoil folds. Despite sharing the structure of the B-chain of ricin, CEL-III binds five Ca^<2＋> ions at five of the six subdomains in both domains 1 and 2. Considering the relatively high similarity among the five subdomains, they are putative binding sites for galactose-related carbohydrates, although it remains to be elucidated whether bound Ca^<2＋> is directly involved in interaction with carbohydrates. The paucity of hydrophobic interactions in the interfaces between the domains and biochemical data suggest that these domains rearrange upon carbohydrate binding in the erythrocyte membrane. This conformational change may be responsible for oligomerization of CEL-III molecules and hemolysis in the erythrocyte membranes.
公開者	American Society for Biochemistry and Molecular Biology
掲載誌名	Journal of Biological Chemistry
巻	279
号	35
開始ページ	37133
終了ページ	37141
刊行年月	2004-08
ISSN	1083351X
pmid	15194688
NCID	AA1202441X
DOI	info:doi/10.1074/jbc.M404065200
URL	http://hdl.handle.net/11094/73650
権利情報	© the American Society for Biochemistry and Molecular Biology.
言語	英語
カテゴリ	学術雑誌論文 Journal Article

著者版フラグ	publisher
NII資源タイプ	学術雑誌論文
ローカル資源タイプ	学術雑誌論文
dcmi資源タイプ	text
DCTERMS.bibliographicCitation	Journal of Biological Chemistry.279(35) P.37133-P.37141
DC.title	Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata : Implications of domain structure for its membrane pore-formation mechanism
DC.creator	Uchida, Tatsuya
	Yamasaki, Takayuki
	Eto, Seiichiro
	Sugawara, Hajime
	Kurisu, Genji
	Nakagawa, Atushi
	Kusunoki, Masami
	Hatakeyama, Tomomitsu
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language" scheme="DCTERMS.RFC1766	英語
DCTERMS.issued" scheme="DCTERMS.W3CDTF	2004-08
DC.identifier	info:doi/10.1074/jbc.M404065200
DC.identifier" scheme="DCTERMS.URI	http://hdl.handle.net/11094/73650
DC.description	This research was originally published in Journal of Biological Chemistry. Tatsuya Uchida, Takayuki Yamasaki, Seiichiro Eto, Hajime Sugawara, Genji Kurisu, Atsushi Nakagawa, Masami Kusunoki and Tomomitsu Hatakeyama. Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata : Implications of domain structure for its membrane pore-formation mechanism. Journal of Biological Chemistry. 2004; 279, 37133-37141. © the American Society for Biochemistry and Molecular Biology.
DCTERMS.abstract	CEL-III is a Ca^<2＋>＋ -dependent and galactose-specific lectin purified from the sea cucumber, Cucumaria echinata, which exhibits hemolytic and hemagglutinating activities. Six molecules of CEL-III are assumed to oligomerize to form an ion-permeable pore in the cell membrane. We have determined the crystal structure of CEL-III by using single isomorphous replacement aided by anomalous scattering in lead at 1.7 Å resolution. CEL-III consists of three distinct domains as follows: the N-terminal two carbohydrate-binding domains (1 and 2), which adopt β-trefoil folds such as the B-chain of ricin and are members of the (QXW)_3 motif family; and domain 3, which is a novel fold composed of two α-helices and one β-sandwich. CEL-III is the first Ca^<2＋> -dependent lectin structure with two β-trefoil folds. Despite sharing the structure of the B-chain of ricin, CEL-III binds five Ca^<2＋> ions at five of the six subdomains in both domains 1 and 2. Considering the relatively high similarity among the five subdomains, they are putative binding sites for galactose-related carbohydrates, although it remains to be elucidated whether bound Ca^<2＋> is directly involved in interaction with carbohydrates. The paucity of hydrophobic interactions in the interfaces between the domains and biochemical data suggest that these domains rearrange upon carbohydrate binding in the erythrocyte membrane. This conformational change may be responsible for oligomerization of CEL-III molecules and hemolysis in the erythrocyte membranes.
DC.rights	© the American Society for Biochemistry and Molecular Biology.
citation_title	Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata : Implications of domain structure for its membrane pore-formation mechanism
citation_author	Uchida, Tatsuya
	Yamasaki, Takayuki
	Eto, Seiichiro
	Sugawara, Hajime
	Kurisu, Genji
	Nakagawa, Atushi
	Kusunoki, Masami
	Hatakeyama, Tomomitsu
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2004-08
citation_journal_title	Journal of Biological Chemistry
citation_volume	279
citation_issue	35
citation_firstpage	37133
citation_lastpage	37141
citation_issn	1083351X
citation_doi	info:doi/10.1074/jbc.M404065200
citation_pmid	15194688
citation_public_url	http://hdl.handle.net/11094/73650

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