1ADW

PSEUDOAZURIN

1ADW の概要

• エントリーDOI: 10.2210/pdb1adw/pdb
• 分子名称: PSEUDOAZURIN, COPPER (II) ION (3 entities in total)
• 機能のキーワード: copper, electron transport, cuproprotein
• 由来する生物種: Paracoccus pantotrophus
• 細胞内の位置: Periplasm: P80401
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26843.55

構造登録者

Williams, P.A. (登録日: 1997-02-18, 公開日: 1997-05-15, 最終更新日: 2024-05-22)

主引用文献

Williams, P.A.,Fulop, V.,Leung, Y.C.,Chan, C.,Moir, J.W.,Howlett, G.,Ferguson, S.J.,Radford, S.E.,Hajdu, J.
Pseudospecific docking surfaces on electron transfer proteins as illustrated by pseudoazurin, cytochrome c550 and cytochrome cd1 nitrite reductase.
Nat.Struct.Biol., 2:975-982, 1995

PubMed Abstract: The structure of pseudoazurin from Thiosphaera pantotropha has been determined and compared to structures of both soluble and membrane-bound periplasmic redox proteins. The results show a matching set of unipolar, but promiscuous, docking motifs based on a positive hydrophobic surface patch on the electron shuttle proteins pseudoazurin and cytochrome c550 and a negative hydrophobic patch on the surface of their known redox partners. The observed electrostatic handedness is argued to be associated with the charge-asymmetry of the membrane-bound components of the redox chain due to von Heijne's 'positives-inside' principle. We propose a 'positives-in-between' rule for electron shuttle proteins, and expect a negative hydrophobic patch to be present on both the highest and lowest redox potential species in a series of electron carriers.

PubMed: 7583671
DOI: 10.1038/nsb1195-975

実験手法

X-RAY DIFFRACTION (2.5 Å)