1new
From Proteopedia
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CYTOCHROME C551.5, NMR, STRUCTURES 1-18 OF 35
Overview
The solution structure of Desulfuromonas acetoxidans cytochrome c7 has, been refined by using 1H-NMR spectra recorded at 800 MHz and by using, pseudocontact shifts in the final energy minimization procedure. The, protein, composed of 68 amino acids, contains three paramagnetic heme, moieties, each with one unpaired electron. The largely distributed, paramagnetism broadens the lines in several protein parts. The structure, is now relatively well resolved all over the backbone by the use of 1315, meaningful NOEs and 90 pseudocontact shifts. The statistical analysis of, the structure indicates its satisfactory quality. The protein-fold is, quite similar to that of the analogous four-heme cytochromes c3 for those, parts which can be considered homologous. The solvent accessibility and, the electrostatic potential surfaces surrounding the three hemes have been, analyzed in terms of their reduction potentials. The resulting magnetic, susceptibility anisotropy data obtained from pseudocontact shifts are, analyzed in terms of structural data.
About this Structure
1NEW is a Single protein structure of sequence from Desulfuromonas acetoxidans with HEC as ligand. This structure superseeds the now removed PDB entry 1CFO. Full crystallographic information is available from OCA.
Reference
800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuromonas acetoxidans., Assfalg M, Banci L, Bertini I, Bruschi M, Turano P, Eur J Biochem. 1998 Sep 1;256(2):261-70. PMID:9760163
Page seeded by OCA on Tue Nov 20 22:12:04 2007
