2L07

1H, 13C, and 15N chemical shifts and structure of brazzein-derived peptide CKR-PNG

2L07 の概要

• エントリーDOI: 10.2210/pdb2l07/pdb
• 関連するPDBエントリー: 2KGQ 2KYQ
• NMR情報: BMRB: 17032
• 分子名称: Defensin-like protein (1 entity in total)
• 機能のキーワード: 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: 2143.38

構造登録者

Dittli, S.M.,Assadi-Porter, F.M.,Rao, H.,Tonelli, M. (登録日: 2010-06-30, 公開日: 2011-06-22, 最終更新日: 2024-10-30)

主引用文献

Dittli, S.M.,Rao, H.,Tonelli, M.,Quijada, J.,Markley, J.L.,Max, M.,Assadi-Porter, F.,Maillet, E.
Structural role of the terminal disulfide bond in the sweetness of brazzein.
Chem Senses, 36:821-830, 2011

PubMed Abstract: Brazzein, a 54 residue sweet-tasting protein, is thought to participate in a multipoint binding interaction with the sweet taste receptor. Proposed sites for interaction with the receptor include 2 surface loops and the disulfide bond that connects the N- and C-termini. However, the importance of each site is not well understood. To characterize the structural role of the termini in the sweetness of brazzein, the position of the disulfide bond connecting the N- and C-termini was shifted by substituting K3-C4-K5 with C3-K4-R5. The apparent affinity and V(max) of the C3-K4-R5-brazzein (CKR-brazzein) variant were only modestly decreased compared with the wild-type (WT) brazzein. We determined a high-resolution structure of CKR-brazzein by nuclear magnetic resonance spectroscopy (backbone root mean square deviation of 0.39 Å). Comparing the structure of CKR-brazzein with that of WT-brazzein revealed that the terminal β-strands of the variant display extended β-structure and increased dynamics relative to WT-brazzein. These results support previous mutagenesis studies and further suggest that, whereas interactions involving the termini are necessary for full function of brazzein, the termini do not constitute the primary site of interaction between brazzein and the sweet taste receptor.

PubMed: 21765060
DOI: 10.1093/chemse/bjr057

実験手法

SOLUTION NMR