Crystal structure of a major seed storage protein, 11S proglobulin, from Amaranthus hypochondriacus: Insight into its physico-chemical properties
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- 作者：Mary Rose T ; ang-Silvas ; Cerrone S. Cabanos ; Laura Denisse Carrazco Pe?a ; Ana Paulina Barba De La Rosa ; Juan Alberto Osuna-Castro ; Shigeru Utsumi ; Bunzo Mikami ; Nobuyuki Maruyama
- 关键词：Amaranthus hypochondriacus ; 11S globulin ; Crystal structure ; Physico-chemical properties
- 刊名：Food Chemistry
- 出版年：2012
- 出版时间：15 November, 2012
- 年：2012
- 卷：135
- 期：2
- 页码：819-826
- 全文大小：2957 K
文摘
Amaranth is a crop known for its high quality proteins. 11S Globulin is one of the most abundant and important storage proteins of the amaranth grain. Here, we report the crystal structure of amaranth 11S proglobulin at a final resolution of 2.28 ?. It belonged to the space group P63 with cell dimensions a = b = 96.6, c = 75.0 ?. It contains one asymmetric unit consisting of 372 residues and 100 water molecules. Disordered regions in the model approximately correspond to the variable regions of the 11S globulins. The structure has an extended ¦Á-helix and ¦Â-barrel domains at both N-terminal and C-terminal regions, which are characteristic of the 11S and 7S globulins. The three dimensional structure suggests that its high thermal stability is due to the cumulative effects of many factors and its good emulsifying property depended on the balance between its surface hydrophobicity and hydrophilicity.