Azurin dimer, crosslinked via disulfide bridge

File:1jvo.gif


1jvo, resolution 2.75Å

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OverviewOverview

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.

About this StructureAbout this Structure

1JVO is a Single protein structure of sequence from Pseudomonas aeruginosa with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Dramatic modulation of electron transfer in protein complexes by crosslinking., van Amsterdam IM, Ubbink M, Einsle O, Messerschmidt A, Merli A, Cavazzini D, Rossi GL, Canters GW, Nat Struct Biol. 2002 Jan;9(1):48-52. PMID:11740504

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