2NRL

Blackfin tuna myoglobin

2NRL の概要

• エントリーDOI: 10.2210/pdb2nrl/pdb
• 関連するPDBエントリー: 2NRM
• 分子名称: Myoglobin, PROTOPORPHYRIN IX CONTAINING FE, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: myoglobin, globin, transport protein
• 由来する生物種: Thunnus atlanticus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16338.75

構造登録者

Schreiter, E.R.,Rodr guez, M.M.,Weichsel, A.,Montfort, W.R.,Bonaventura, J. (登録日: 2006-11-02, 公開日: 2007-05-08, 最終更新日: 2023-08-30)

主引用文献

Schreiter, E.R.,Rodriguez, M.M.,Weichsel, A.,Montfort, W.R.,Bonaventura, J.
S-nitrosylation-induced conformational change in blackfin tuna myoglobin.
J.Biol.Chem., 282:19773-19780, 2007

PubMed Abstract: S-nitrosylation is a post-translational protein modification that can alter the function of a variety of proteins. Despite the growing wealth of information that this modification may have important functional consequences, little is known about the structure of the moiety or its effect on protein tertiary structure. Here we report high-resolution x-ray crystal structures of S-nitrosylated and unmodified blackfin tuna myoglobin, which demonstrate that in vitro S-nitrosylation of this protein at the surface-exposed Cys-10 directly causes a reversible conformational change by "wedging" apart a helix and loop. Furthermore, we have demonstrated in solution and in a single crystal that reduction of the S-nitrosylated myoglobin with dithionite results in NO cleavage from the sulfur of Cys-10 and rebinding to the reduced heme iron, showing the reversibility of both the modification and the conformational changes. Finally, we report the 0.95-A structure of ferrous nitrosyl myoglobin, which provides an accurate structural view of the NO coordination geometry in the context of a globin heme pocket.

PubMed: 17488722
DOI: 10.1074/jbc.M701363200

実験手法

X-RAY DIFFRACTION (0.91 Å)