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Related Experiment Videos

On cytochrome c3 folding.

Y Higuchi, M Kusunoki, N Yasuoka

    Journal of Biochemistry
    |December 1, 1981
    PubMed
    Summary
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    Structural analysis of cytochrome c3 from Desulfovibrio vulgaris Miyazaki (DvM) reveals similarities and differences with D. desulfuricans Norway (DdN). A revised sequence alignment highlights 24 conserved residues crucial for folding.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Microbiology

    Background:

    • Cytochromes c3 are essential electron carriers in sulfate-reducing bacteria.
    • Understanding their structure is key to elucidating their function in electron transfer pathways.

    Purpose of the Study:

    • To perform a detailed structural comparison of cytochrome c3 from Desulfovibrio vulgaris Miyazaki (DvM) and Desulfovibrio desulfuricans Norway (DdN).
    • To revise the sequence alignment of the cytochrome c3 family based on structural insights.

    Main Methods:

    • Detailed scrutiny of the main chain folding and heme group arrangement in DvM cytochrome c3.
    • Comparative analysis of DvM and DdN cytochrome c3 structures, focusing on residue disposition and surface loop conformations.

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    Main Results:

    • The relative arrangement of heme groups and the binding residues (cysteine and histidine) are highly conserved between DvM and DdN cytochrome c3.
    • Distinct structural variations were observed in the surface loops of the two proteins.
    • A revised sequence alignment incorporating 24 evolutionarily conserved residues was proposed.

    Conclusions:

    • The conserved residues identified are likely critical for maintaining the characteristic folding pattern of cytochromes c3.
    • Structural comparisons provide a refined basis for understanding cytochrome c3 evolution and function.