1C53
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
Summary for 1C53
Entry DOI | 10.2210/pdb1c53/pdb |
Descriptor | CYTOCHROME C553, PROTOPORPHYRIN IX CONTAINING FE (2 entities in total) |
Functional Keywords | electron transport |
Biological source | Desulfovibrio vulgaris str. 'Miyazaki F' |
Cellular location | Periplasm: P00120 |
Total number of polymer chains | 1 |
Total formula weight | 9028.15 |
Authors | Nakagawa, A.,Higuchi, Y.,Yasuoka, N.,Katsube, Y.,Yaga, T. (deposition date: 1991-08-26, release date: 1993-10-31, Last modification date: 2024-02-07) |
Primary citation | Nakagawa, A.,Higuchi, Y.,Yasuoka, N.,Katsube, Y.,Yagi, T. 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. J.Biochem.(Tokyo), 108:701-703, 1990 Cited by PubMed Abstract: 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. PubMed: 1964450PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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