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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC00663
Cytochrome c oxidase subunit Vb family signature and profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC00663

Description

Cytochrome c oxidase (EC 1.9.3.1) [1] is an oligomeric enzymatic complex which is a component of the respiratory chain complex and is involved in the transfer of electrons from cytochrome c to oxygen. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plasma membrane. In addition to the three large subunits that form the catalytic center of the enzyme complex there are, in eukaryotes, a variable number of small polypeptidic subunits. One of these subunits which is known as Vb in mammals, V in slime mold and IV in yeast, binds a zinc atom. The sequence of subunit Vb is well conserved and includes three to four conserved cysteines that coordinate the zinc ion [2,3]. Two of these cysteines are clustered in the C-terminal section of the subunit; we have used this region as a signature pattern. We also developed a profile that covers the whole subunit Vb zinc binding region.

Last update:

January 2008 / Text revised; profile added.

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Technical section

PROSITE methods (with tools and information) covered by this documentation:

COX5B_2, PS51359; Cytochrome c oxidase subunit Vb, zinc binding domain profile  (MATRIX)

COX5B_1, PS00848; Cytochrome c oxidase subunit Vb, zinc binding region signature  (PATTERN)


References

1AuthorsCapaldi R.A. Malatesta F. Darley-Usmar V.M.
TitleStructure of cytochrome c oxidase.
SourceBiochim. Biophys. Acta 726:135-148(1983).
PubMed ID6307356

2AuthorsRizzuto R. Sandona D. Brini M. Capaldi R.A. Bisson R.
TitleThe most conserved nuclear-encoded polypeptide of cytochrome c oxidase is the putative zinc-binding subunit: primary structure of subunit V from the slime mold Dictyostelium discoideum.
SourceBiochim. Biophys. Acta 1129:100-104(1991).
PubMed ID1661610

3AuthorsTsukihara T. Aoyama H. Yamashita E. Tomizaki T. Yamaguchi H. Shinzawa-Itoh K. Nakashima R. Yaono R. Yoshikawa S.
TitleThe whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A.
SourceScience 272:1136-1144(1996).
PubMed ID8638158



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