6533b827fe1ef96bd1285b9b
RESEARCH PRODUCT
Metal coordination of azurin in the unfolded state.
Antonio DonaireCarmen RomeroJosé M. Moratalsubject
Protein FoldingBlue copper proteinProtein ConformationRack mechanismBiophysicschemistry.chemical_elementLigandsBiochemistryNuclear magnetic resonanceMetalParamagnetismProtein structureStructural BiologyAzurinNickelGeneticsMolecular BiologyNuclear Magnetic Resonance BiomolecularGuanidineBinding SitesCell BiologyCobaltCrystallographyNickelchemistryvisual_artPseudomonas aeruginosaProton NMRvisual_art.visual_art_mediumProtein foldingAzurinProtonsCobaltdescription
Abstract1H NMR data applied to the paramagnetic cobalt(II) derivative of azurin from Pseudomonas aeruginosa have made it possible to show that the metal ion is bound to the protein in the unfolded state. The relaxation data as well as the low magnetic anisotropy of the metal ion indicate that the cobalt ion is tetrahedral in the unfolded form. The cobalt ligands have been identified as the residues Gly45, His46, Cys112 and His117. Met121 is not coordinated in the unfolded state. In this state, the metal ion is not constrained to adopt a bipyramidal geometry, as imposed by the protein when it is folded. This is clear confirmation of the rack-induced bonding mechanism previously proposed for the metal ion in azurin.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1998-11-27 | FEBS letters |