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.
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.
Nakagawa
A
A
Photon Factory, National Laboratory for High Energy Physics, Hyogo.
Higuchi
Y
Y
Yasuoka
N
N
Katsube
Y
Y
Yagi
T
T
D000595:Amino Acid Sequence; D003574:Cytochrome c Group / Q000737:chemistry* / Q000145:classification / Q000235:genetics; D003901:Desulfovibrio / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D010802:Phylogeny; D011487:Protein Conformation; D014961:X-Ray Diffraction
D003574:Cytochrome c Group; C083951:cytochrome c553; C022302:cytochrome C-552