2FTA

Structure of Cu(II)azurin with the metal-binding loop sequence "CTFPGHSALM" replaced with "CTPHPFM"

2FTA の概要

• エントリーDOI: 10.2210/pdb2fta/pdb
• 関連するPDBエントリー: 2FT6 2FT7 2FT8
• 分子名称: Azurin, COPPER (II) ION, NONAETHYLENE GLYCOL, ... (6 entities in total)
• 機能のキーワード: blue copper-binding protein, greek-key beta-barrel, 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: 4
• 化学式量合計: 56249.68

構造登録者

Banfield, M.J. (登録日: 2006-01-24, 公開日: 2006-04-11, 最終更新日: 2023-08-30)

主引用文献

Li, C.,Yanagisawa, S.,Martins, B.M.,Messerschmidt, A.,Banfield, M.J.,Dennison, C.
Basic requirements for a metal-binding site in a protein: The influence of loop shortening on the cupredoxin azurin.
Proc.Natl.Acad.Sci.Usa, 103:7258-7263, 2006

PubMed Abstract: The main active-site loop of the copper-binding protein azurin (a cupredoxin) has been shortened from C(112)TFPGH(117)SALM(121) to C(112)TPH(115)PFM(118) (the native loop from the cupredoxin amicyanin) and also to C(112)TPH(115)PM(117). The Cu(II) site structure is almost unaffected by shortening, as is that of the Cu(I) center at alkaline pH in the variant with the C(112)TPH(115)PM(117) loop sequence. Subtle spectroscopic differences due to alterations in the spin density distribution at the Cu(II) site can be attributed mainly to changes in the hydrogen-bonding pattern. Electron transfer is almost unaffected by the introduction of the C(112)TPH(115)PFM(118) loop, but removal of the Phe residue has a sizable effect on reactivity, probably because of diminished homodimer formation. At mildly acidic pH values, the His-115 ligand protonates and dissociates from the cuprous ion, an effect that has a dramatic influence on the reactivity of cupredoxins. These studies demonstrate that the amicyanin loop adopts a conformation identical to that found in the native protein when introduced into azurin, that a shorter than naturally occurring C-terminal active-site loop can support a functional T1 copper site, that CTPHPM is the minimal loop length required for binding this ubiquitous electron transfer center, and that the length and sequence of a metal-binding loop regulates a range of structural and functional features of the active site of a metalloprotein.

PubMed: 16651527
DOI: 10.1073/pnas.0600774103

実験手法

X-RAY DIFFRACTION (1.61 Å)