3. 新しいタンパク質立体構造 ニワトリ卵黄膜由来の蛋白質VMO-1の結晶構造解析 Crystal Structure of VMO-I (Vitelline Membrane Outer Layer Protein I) Isolated from the Vitelline Membrane of Hen's Eggs

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The crystal structure of vitelline membrane outer layer protein I (VMO-I), which was isolated from the outer layer of the vitelline membrane of hen's eggs, has been determined by X-ray analysis. VMO-I is composed of three homologous structures, each containing a β-sheet forming Greek key motif, which are in accordance with the three repeats in the sequence. These three homologous structures are related by a pseudo three-fold symmetry. This new folding motif, recently designated as the β-prism, has also been observed in the second domain of δ-endotoxin. Thus, VMO-I and δ-endotoxin constitute a new family with a novel folding motif. The VMO-I molecule has a groove-like cavity. This region contains invariant acidic residues in the three repeats. VMO-I is assumed to be an oligosaccharide binding protein like lysozyme, although details of its catalytic function remain to be solved. A docking model of an oligosaccharide to VMO-I has been constructed. This model shows that the cavity has a sufficient space to bind roughly pentamer saccharides. The structural features strongly suggest that the negatively-charged cavity in the top region of the protein may be involved in an unknown catalytic reaction.

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  • 日本結晶学会誌  

    日本結晶学会誌 38(1), 68-72, 1996-02-28 

    The Crystallographic Society of Japan

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各種コード

  • NII論文ID(NAID)
    10002024783
  • NII書誌ID(NCID)
    AN00188364
  • 本文言語コード
    JPN
  • 資料種別
    ART
  • ISSN
    03694585
  • NDL 記事登録ID
    3934773
  • NDL 雑誌分類
    ZM46(科学技術--地球科学--岩石・鉱物・鉱床)
  • NDL 請求記号
    Z15-138
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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