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4HE7

Crystal Structure of Brazzein

4HE7 の概要
エントリーDOI10.2210/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: 23519673
DOI: 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)
構造検証レポート
Validation report summary of 4he7
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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