1JVL

Azurin dimer, covalently crosslinked through bis-maleimidomethylether

Summary for 1JVL

• Entry DOI: 10.2210/pdb1jvl/pdb
• Descriptor: Azurin, COPPER (II) ION, NICKEL (II) ION, ... (6 entities in total)
• Functional Keywords: cupredoxin, electron transfer, covalent crosslink, electron transport
• Biological source: Pseudomonas aeruginosa
• Cellular location: Periplasm: P00282
• Total number of polymer chains: 2
• Total formula weight: 28626.62

Authors

van Amsterdam, I.M.C.,Ubbink, M.,Einsle, O.,Messerschmidt, A.,Merli, A.,Cavazzini, D.,Rossi, G.L.,Canters, G.W. (deposition date: 2001-08-30, release date: 2002-01-04, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)