1s05
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NMR-validated structural model for oxidized R.palustris cytochrome c556
OverviewOverview
The structure of oxidized Rhodopseudomonas palustris cytochrome c(556) 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.
About this StructureAbout this Structure
1S05 is a Single protein structure of sequence from Rhodopseudomonas palustris with HEM as ligand. Full crystallographic information is available from OCA.
ReferenceReference
NMR-validated structural model for oxidized Rhodopseudomonas palustris cytochrome c(556)., Bertini I, Faraone-Mennella J, Gray HB, Luchinat C, Parigi G, Winkler JR, J Biol Inorg Chem. 2004 Mar;9(2):224-30. Epub 2004 Jan 20. PMID:14735333
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