1c53
From Proteopedia
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S-CLASS CYTOCHROMES C HAVE A VARIETY OF FOLDING PATTERNS: STRUCTURE OF CYTOCHROME C-553 FROM DESULFOVIBRIO VULGARIS DETERMINED BY THE MULTI-WAVELENGTH ANOMALOUS DISPERSION METHOD
Overview
The three-dimensional structure of cytochrome c-553 isolated from, sulfate-reducing bacterium, Desulfovibrio vulgaris Miyazaki F strain, has, been determined by the multi-wavelength anomalous dispersion technique, with use of synchrotron radiation. The result shows that bacterial S-class, cytochromes c have a variety of folding patterns. The relative location of, two a-helices at amino- and carboxyl-terminals and the style of bonding to, the heme group show "cytochrome c folding," but other regions of the, structure are different from those of other cytochromes c previously, reported. The results also give useful information about the location of, sulfate-reducing bacterium on the phylogenetic tree of the bacterial, cytochromes c superfamily.
About this Structure
1C53 is a Single protein structure of sequence from Desulfovibrio vulgaris with HEM as ligand. Full crystallographic information is available from OCA.
Reference
S-class cytochromes c have a variety of folding patterns: structure of cytochrome c-553 from Desulfovibrio vulgaris determined by the multi-wavelength anomalous dispersion method., Nakagawa A, Higuchi Y, Yasuoka N, Katsube Y, Yagi T, J Biochem (Tokyo). 1990 Nov;108(5):701-3. PMID:1964450
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