3N2J

Azurin H117G, oxidized form

3N2J の概要

• エントリーDOI: 10.2210/pdb3n2j/pdb
• 関連するPDBエントリー: 4AZU
• 分子名称: Azurin, COPPER (II) ION (3 entities in total)
• 機能のキーワード: copper proteins, electron transfer, pseudo-translation, 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: 12
• 化学式量合計: 168093.55

構造登録者

Hoffmann, M.,Alagaratnam, S.,Canters, G.W.,Einsle, O. (登録日: 2010-05-18, 公開日: 2011-04-06, 最終更新日: 2024-10-16)

主引用文献

Alagaratnam, S.,Meeuwenoord, N.J.,Navarro, J.A.,Hervas, M.,De la Rosa, M.A.,Hoffmann, M.,Einsle, O.,Ubbink, M.,Canters, G.W.
Probing the reactivity of different forms of azurin by flavin photoreduction.
Febs J., 278:1506-1521, 2011

PubMed Abstract: The reactivity of a variant of the blue copper protein, azurin from Pseudomonas aeruginosa, was investigated with laser flash photolysis and compared with the reactivity of the wild-type (WT) protein. The variant was obtained by changing the Cu ligating His117 for a glycine. The mutation creates a gap in the ligand shell of the Cu that can be filled with external ligands or water molecules. The crystal structure of the H117G variant is reported. It shows that the immediate surrounding of the Cu site in the variant exhibits less rigidity than in the WT protein and that the loop containing the Cu ligands Cys112, His117 and Met121 in the WT protein has gained flexibility in the H117G variant. Flash photolysis experiments were performed with 5-deazariboflavin and 8α-imidazolyl-(N-propylyl)-amino riboflavin as electron donors to probe the reactivity of WT and H117G azurin, and of H117G azurin for which the gap in the Cu co-ordination shell was filled with imidazole. 8α-Imidazolyl-(N-propylyl)-amino riboflavin appears one to two orders less efficient as a photo-flash reductant than 5-deazariboflavin. The reactivity of the H117G variant in the absence of external ligands appears to be 2.5-fold lower than the WT reactivity (second-order rate constants of 51 ± 2 × 10(7) m(-1) ·s(-1) versus 21 ± 1 × 10(7) m(-1) ·s(-1) ), whereas the addition of imidazole restores reactivity to above the WT level (71 ± 4 × 10(7) m(-1) ·s(-1) ). The differences are discussed in terms of structural modifications and changes in reorganizational energy and electronic coupling. Database Structural data are available in the Protein Data Bank under the accession number 3N2J.

PubMed: 21352498
DOI: 10.1111/j.1742-4658.2011.08067.x

実験手法

X-RAY DIFFRACTION (1.35 Å)