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PROSITE documentation PDOC00177 [for PROSITE entry PS51296]

Rieske [2Fe-2S] iron-sulfur domain profile





Description

There are multiple types of iron-sulfur clusters which are grouped into three main categories based on their atomic content: [2Fe-2S], [3Fe-4S], [4Fe-4S] (see <PDOC00176>), and other hybrid or mixed metal types. Two general types of [2Fe-2S] clusters are known and they differ in their coordinating residues. The ferredoxin-type [2Fe-2S] clusters are coordinated to the protein by four cysteine residues (see <PDOC00175>). The Rieske-type [2Fe-2S] cluster is coordinated to its protein by two cysteine residues and two histidine residues [1,2].

The structure of several Rieske domains has been solved (see for example <PDB:1RIE>) [3]. It contains three layers of antiparallel β sheets forming two β sandwiches. Both β sandwiches share the central sheet 2. The metal-binding site is at the top of the β sandwich formed by the sheets 2 and 3. The Fe1 iron of the Rieske cluster is coordinated by two cysteines while the other iron Fe2 is coordinated by two histidines. Two inorganic sulfide ions bridge the two iron ions forming a flat, rhombic cluster.

Rieske-type iron-sulfur clusters are common to electron transfer chains of mitochondria and chloroplast and to non-heme iron oxygenase systems:

  • The Rieske protein of the Ubiquinol-cytochrome c reductase (EC 1.10.2.2) (also known as the bc1 complex or complex III), a complex of the electron transport chains of mitochondria and of some aerobic prokaryotes; it catalyzes the oxidoreduction of ubiquinol and cytochrome c.
  • The Rieske protein of chloroplastic plastoquinone-plastocyanin reductase (EC 1.10.99.1) (also known as the b6f complex). It is functionally similar to the bc1 complex and catalyzes the oxidoreduction of plastoquinol and cytochrome f.
  • Bacterial naphthalene 1,2-dioxygenase subunit α, a component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-naphthalene dihydrodiol.
  • Bacterial 3-phenylpropionate dioxygenase ferredoxin subunit.
  • Bacterial toluene monoxygenase.
  • Bacterial biphenyl dioxygenase.

The profile we developed covers the whole Rieske domain.

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

Last update:

March 2007 / Text revised; profiles added; patterns deleted.

Note:

The Rieske profile is in competition with a profile of a related domain, i.e. nirD Rieske-like domain (see <PDOC51300>).

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Technical section

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

RIESKE, PS51296; Rieske [2Fe-2S] iron-sulfur domain profile  (MATRIX)


References

1AuthorsFerraro D.J. Gakhar L. Ramaswamy S.
TitleRieske business: structure-function of Rieske non-heme oxygenases.
SourceBiochem. Biophys. Res. Commun. 338:175-190(2005).
PubMed ID16168954
DOI10.1016/j.bbrc.2005.08.222

2AuthorsSchneider D. Schmidt C.L.
TitleMultiple Rieske proteins in prokaryotes: where and why?
SourceBiochim. Biophys. Acta 1710:1-12(2005).
PubMed ID16271700
DOI10.1016/j.bbabio.2005.09.003

3AuthorsIwata S. Saynovits M. Link T.A. Michel H.
TitleStructure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 A resolution.
SourceStructure 4:567-579(1996).
PubMed ID8736555



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

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