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|Titolo:||NMR-validated structural model for oxidized Rhodopseudomonas palustris cytochrome c556|
|Autori interni:||BERTINI, IVANO|
|Data di pubblicazione:||2004|
|Abstract:||The structure of oxidized Rhodopseudomonas palustris cytochrome c556 has been modeled after that of high-spin cytochrome c¢ from the same bacterium, the latter being the protein with the greatest sequence identity (35%) among all sequenced proteins in the genomes. The two proteins differ in the number of ligands to iron and in spin state, the former being six-coordinate low-spin and the latter five-coordinate high-spin. In order to validate this modeled structure, several structural restraints were obtained by performing a restricted set of NMR experiments, without performing a complete assignment of the protein signals. The aim was to exploit the special restraints arising from the paramagnetism of the metal ion. A total of 43 residual-dipolar-coupling and 74 pseudocontact-shift restraints, which together sampled all regions of the protein, were used in conjunction with over 40 routinely obtained NOE distance restraints. A calculation procedure was undertaken combining the program MODELLER and the solution structure determination program PARAMAGNETIC DYANA, which includes paramagnetism-based restraints. The directions and magnitude of the magnetic susceptibility anisotropy tensor were also calculated. The approach readily provides useful results, especially for paramagnetic metalloproteins of moderate to large dimensions.|
|Appare nelle tipologie:||1a - Articolo su rivista|
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