2HX7

Crystal structure of Cu(II) Azurin with the metal-binding loop sequence "CTFPGHSALM" replaced with "CSPHQGAGM"

2HX7 の概要

• エントリーDOI: 10.2210/pdb2hx7/pdb
• 関連するPDBエントリー: 2FT6 2FT7 2FT8 2FTA
• 分子名称: Azurin, COPPER (II) ION (3 entities in total)
• 機能のキーワード: blue copper-binding protein, greek-key beta-barrel, loop mutagenesis, 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: 27698.18

構造登録者

Banfield, M.J. (登録日: 2006-08-03, 公開日: 2007-01-30, 最終更新日: 2024-11-20)

主引用文献

Li, C.,Banfield, M.J.,Dennison, C.
Engineering Copper Sites in Proteins: Loops Confer Native Structures and Properties to Chimeric Cupredoxins.
J.Am.Chem.Soc., 129:709-718, 2007

PubMed Abstract: The ligand-containing loops of two copper-binding electron-transfer proteins (cupredoxins) have been swapped. In the azurin (AZ) variant in which the plastocyanin (PC) sequence is introduced (AZPC), the loop adopts a conformation identical to that in PC. The reduction potential of AZPC is raised as compared to AZ and matches that of PC. In the previously published AZAMI variant (AMI = amicyanin), the shorter introduced loop adopts the same conformation as in AMI, and the reduction potential is lowered to equal that of AMI (Yanagisawa, S.; Dennison, C. J. Am. Chem. Soc. 2004, 126, 15711-15719. Li, C.; et al. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 7258-7263). Thus, the loop structure plays an important role in tuning the reduction potential of a type 1 copper site with contributions from protein dipoles in this region probably the most important feature. The structure of the loop also seems to be a major factor in controlling dissociation and protonation of the C-terminal His ligand, which can act as a switch to regulate electron-transfer reactivity. The PCAZ variant (PC with the AZ loop) possesses an active site, which is different from those of both PC and AZ, and it is assumed that the introduced loop does not adopt a structure as in AZ. This contributes to the observed instability of PCAZ and highlights that loop-scaffold interactions are important for stabilizing the active site of a cupredoxin.

PubMed: 17227035
DOI: 10.1021/ja0661562

実験手法

X-RAY DIFFRACTION (1.55 Å)