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.

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.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Nakagawa A,Higuchi Y,Yasuoka N,Katsube Y,Yagi T

doi

10.1093/oxfordjournals.jbchem.a123267

subject

Has Abstract

pub_date

1990-11-01 00:00:00

pages

701-3

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

108

pub_type

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