Structural, dynamical and functional aspects of the inner motions in the blue copper protein azurin (Articolo in rivista)

Type
Label
  • Structural, dynamical and functional aspects of the inner motions in the blue copper protein azurin (Articolo in rivista) (literal)
Anno
  • 2007-01-01T00:00:00+01:00 (literal)
Alternative label
  • Rizzuti, B; Sportelli, L; Guzzi, R (2007)
    Structural, dynamical and functional aspects of the inner motions in the blue copper protein azurin
    in Biophysical chemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Rizzuti, B; Sportelli, L; Guzzi, R (literal)
Pagina inizio
  • 532 (literal)
Pagina fine
  • 539 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 125 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Univ Calabria, Dipartimento Fis, Lab Biofis Mol, I-87036 Arcavacata Di Rende, Italy; Univ Calabria, Dipartimento Fis, Lab Licryl, CNR,INFM, I-87036 Arcavacata Di Rende, Italy (literal)
Titolo
  • Structural, dynamical and functional aspects of the inner motions in the blue copper protein azurin (literal)
Abstract
  • Molecular dynamics was applied to dissect out the internal motions of azurin, a copper protein performing electron transfer. Simulations of 16.5 ns were analyzed in search of coordinated displacements of amino acid residues that are important for the protein function. A region with high conformational instability was found in the 'southern' end of the molecule, far away from the copper site and the binding sites for the redox partners of azurin. By excluding the 'southern' region from the subsequent analysis, correlated motions were identified in the hydrophobic patch that surrounds the protein active site. The simulation results are in excellent agreement with recent NMR data on azurin in solution [A. V Zhuravleva, D. M. Korzhnev, E. Kupce, A. S. Arseniev, M. Billeter, V. Y. Orekhov, Gated electron transfers and electron pathways in azurin: a NMR dynamic study at multiple fields and temperatures, J. Mol. Biol. 342 (2004) 1599-1611] and suggest a rationale for cooperative displacements of protein residues that are thought to be critical for the electron transfer process. A number of other structural and dynamic features of azurin are discussed in the context of the blue copper protein family and an explanation is proposed to account for the variability/conservation of some regions in the cupredoxins. (c) 2006 Elsevier B.V. All rights reserved. (literal)
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