1JVL

Azurin dimer, covalently crosslinked through bis-maleimidomethylether

1JVL の概要

• エントリーDOI: 10.2210/pdb1jvl/pdb
• 分子名称: Azurin, COPPER (II) ION, NICKEL (II) ION, ... (6 entities in total)
• 機能のキーワード: cupredoxin, electron transfer, covalent crosslink, 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: 28626.62

構造登録者

van Amsterdam, I.M.C.,Ubbink, M.,Einsle, O.,Messerschmidt, A.,Merli, A.,Cavazzini, D.,Rossi, G.L.,Canters, G.W. (登録日: 2001-08-30, 公開日: 2002-01-04, 最終更新日: 2024-10-30)

主引用文献

van Amsterdam, I.M.C.,Ubbink, M.,Einsle, O.,Messerschmidt, A.,Merli, A.,Cavazzini, D.,Rossi, G.L.,Canters, G.W.
Dramatic modulation of electron transfer in protein complexes by crosslinking
Nat.Struct.Biol., 9:48-52, 2002

PubMed Abstract: The transfer of electrons between proteins is an essential step in biological energy production. Two protein redox partners are often artificially crosslinked to investigate the poorly understood mechanism by which they interact. To better understand the effect of crosslinking on electron transfer rates, we have constructed dimers of azurin by crosslinking the monomers. The measured electron exchange rates, combined with crystal structures of the dimers, demonstrate that the length of the linker can have a dramatic effect on the structure of the dimer and the electron transfer rate. The presence of ordered water molecules in the protein-protein interface may considerably influence the electronic coupling between redox centers.

PubMed: 11740504
DOI: 10.1038/nsb736

実験手法

X-RAY DIFFRACTION (2 Å)