1k3h
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NMR Solution Structure of Oxidized Cytochrome c-553 from Bacillus pasteurii
OverviewOverview
The solution structure of oxidized cytochrome c(553) (71 amino acid, residues) from the Gram-positive bacterium Bacillus pasteurii is here, reported and compared with the available crystal structure. The solution, structure is obtained from 1609 meaningful NOE data (22.7 per residue), 76, dihedral angles, and 59 pseudocontact shifts. The root mean square, deviations from the average structure are 0.25+/-0.07 and 0.59+/-0.13 A, for the backbone and all heavy atoms, respectively, and the quality, assessment of the structure is satisfactory. The solution structure, closely reproduces the fold observed in the crystal structure. The, backbone mobility was then investigated through amide (15)N relaxation, rate and (15)N-(1)H NOE measurements. The protein is rigid in both the, sub-nanosecond and millisecond time scales, probably due to the relatively, large heme:number of amino acids ratio. Modeling of eight c-type, cytochromes from other Gram-positive bacteria with a high sequence, identity (>30 %) to the present cytochrome c(553) was performed. Analysis, of consensus features accounts for the relatively low reduction potential, as being due to extensive heme hydration and indicates residues 34-35, 44-46, 69-72, and 75 as a conserved hydrophobic patch for the interaction, with a protein partner. At variance with mitochondrial c-type cytochrome, this protein does not experience pH-dependent coordination equilibria. The, reasons for this difference are analyzed.
About this StructureAbout this Structure
1K3H is a Single protein structure of sequence from Sporosarcina pasteurii with HEC as ligand. Full crystallographic information is available from OCA.
ReferenceReference
NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteria., Banci L, Bertini I, Ciurli S, Dikiy A, Dittmer J, Rosato A, Sciara G, Thompsett AR, Chembiochem. 2002 Apr 2;3(4):299-310. PMID:11933230
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