書誌事項
- タイトル別名
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- Structural Basis of the Phospholipase C Activity in Neutral Sphingomyelinase from Bacillus cereus.
- Bacillus cereus ユライ スフィンゴミエリナーゼ ノ Xセン ケッショウ コウゾウ カイセキ
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Degradation of cell membrane and mucosa, of which phospholipads are major components, and production of lipid mediators are roles of phospholipases from pathogenic bacteria to grow, survive and spread in the host organism. The studies on the enzymes are important for the pathobiology of bacterial infectious disease. The crystal structure of Sphingomyelinase from Bacillus cereus revealed the structure basis of the phospholipase C and hemolysis activities in a divalent cation dependent manner. The water-bridged double divalent cations were concluded to be the catalytic architecture to the phospholipase C activity. In addition, the β-hairpin structure with aromatic amino acid residues was shown to be involved in the membrane binding of the enzyme as a part of the hemolysis activity.
収録刊行物
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- 日本結晶学会誌
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日本結晶学会誌 49 (3), 198-205, 2007
日本結晶学会
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詳細情報 詳細情報について
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- CRID
- 1390001204087504512
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- NII論文ID
- 10019748235
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- NII書誌ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL書誌ID
- 8880074
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可