4HE7
Crystal Structure of Brazzein
4HE7 の概要
| エントリーDOI | 10.2210/pdb4he7/pdb |
| 分子名称 | Defensin-like protein, SODIUM ION (3 entities in total) |
| 機能のキーワード | sweet-tasting protein, plant protein |
| 由来する生物種 | Pentadiplandra brazzeana |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 6514.32 |
| 構造登録者 | Nagata, K.,Hongo, N.,Kameda, Y.,Yamamura, A.,Sasaki, H.,Lee, W.C.,Ishikawa, K.,Suzuki, E.,Tanokura, M. (登録日: 2012-10-03, 公開日: 2013-03-27, 最終更新日: 2024-11-20) |
| 主引用文献 | Nagata, K.,Hongo, N.,Kameda, Y.,Yamamura, A.,Sasaki, H.,Lee, W.C.,Ishikawa, K.,Suzuki, E.,Tanokura, M. The structure of brazzein, a sweet-tasting protein from the wild African plant Pentadiplandra brazzeana Acta Crystallogr.,Sect.D, 69:642-647, 2013 Cited by PubMed Abstract: Brazzein is the smallest sweet-tasting protein and was isolated from the wild African plant Pentadiplandra brazzeana. The brazzein molecule consists of 54 amino-acid residues and four disulfide bonds. Here, the first crystal structure of brazzein is reported at 1.8 Å resolution and is compared with previously reported solution structures. Despite the overall structural similarity, there are several remarkable differences between the crystal and solution structures both in their backbone folds and side-chain conformations. Firstly, there is an additional α-helix in the crystal structure. Secondly, the atomic r.m.s.d.s between the corresponding C(α)-atom pairs are as large as 2.0-2.2 Å between the crystal and solution structures. Thirdly, the crystal structure exhibits a molecular shape that is similar but not identical to the solution structures. The crystal structure of brazzein reported here will provide additional information and further insights into the intermolecular interaction of brazzein with the sweet-taste receptor. PubMed: 23519673DOI: 10.1107/S0907444913001005 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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