3U25

Crystal structure of P. aeruginoas azurin containing a Tyr-His hydrogen bonded pair

3U25 の概要

• エントリーDOI: 10.2210/pdb3u25/pdb
• 分子名称: Azurin, COPPER (II) ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• 機能のキーワード: azurin, cupredoxin, electron transport
• 由来する生物種: Pseudomonas aeruginosa
• 細胞内の位置: Periplasm: P00282
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28092.73

構造登録者

Warren, J.J.,Winkler, J.R.,Gray, H.B. (登録日: 2011-09-30, 公開日: 2011-12-28, 最終更新日: 2024-10-16)

主引用文献

Warren, J.J.,Winkler, J.R.,Gray, H.B.
Redox properties of tyrosine and related molecules.
Febs Lett., 586:596-602, 2012

PubMed Abstract: Redox reactions of tyrosine play key roles in many biological processes, including water oxidation and DNA synthesis. We first review the redox properties of tyrosine (and other phenols) in small molecules and related polypeptides, then report work on (H20)/(Y48)-modified Pseudomonas aeruginosa azurin. The crystal structure of this protein (1.18Å resolution) shows that H20 is strongly hydrogen bonded to Y48 (2.7-2.8Å tyrosine-O to histidine-N distance). A firm conclusion is that proper tuning of the tyrosine potential by a proton-accepting base is critical for biological redox functions.

PubMed: 22210190
DOI: 10.1016/j.febslet.2011.12.014

実験手法

X-RAY DIFFRACTION (1.18 Å)