title: Nuclear magnetic resonance signal chemical shifts and molecular simulations: a multidisciplinary approach to modeling copper protein structures.
abstract: Nuclear magnetic resonance (NMR) chemical shifts are experimental observables that are available during the first stage of the protein structure determination process. Recently, some methodologies for building structural models of proteins using only these experimental data have been implemented. To assess the potential of these methods for modeling metalloproteins (generally considered a challenging benchmark), we determined the structures of the yeast copper chaperone Atx1 and the CuA domain of Thermus thermophilus cytochrome c oxidase starting from the available chemical shift data. The metal centers were modeled using molecular dynamics simulations with molecular mechanics potentials. The results obtained are evaluated and discussed.
authors.affiliation: Magnetic Resonance Center (CERM) and Department of Chemistry Ugo Schiff, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy.
authors.forename: Jacopo
authors.initials: J
authors.lastname: Sgrignani
authors.forename: Roberta
authors.initials: R
authors.lastname: Pierattelli
mesh_terms: D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D003300:Copper / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D003574:Cytochrome c Group / Q000737:chemistry* / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism; D016963:Thermus thermophilus / Q000201:enzymology
chemical_list: C093341:ATX1 protein, S cerevisiae; D002352:Carrier Proteins; D003574:Cytochrome c Group; D029701:Saccharomyces cerevisiae Proteins; D003300:Copper