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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.
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Amos Bairoch

PROSITE documentation PDOC51839
His(Cys)3-ligated-type [4Fe-4S] domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC51839

Description

The following proteins contain a His(Cys)3-ligated-type [4Fe-4S] domain that consists of just two α helices separated by a loop region that coordinates a [4Fe-4S] cluster through an unusual H-x(3)-C-x(2)-C-x(5)-C motif that includes one His and three Cys residues (see <PDB:1FEH>) [1,2,3,4,5,6]:

  • Prokaryotic and mitochondrial NuoG/Nqo3 subunit (75 kDa) of NADH:ubiquinone oxidoreductase (complex I) (see <PDOC00554>).
  • Clostridium pasteurianum of the iron-only hydrogenase (CpI) (EC:1.12.7.2).
  • Ralstonia eutropha NAD-dependent formate dehydrogenase α subunit (FdsA).
  • Moorella thermoacetica formate dehydrogenase α subunit (FdhA).
  • Desulfovibrio fructosivorans NADP-reducing hydrogenase subunit HndD.
  • Clostridium pasteurianum
  • Ralstonia eutropha NAD-reducing [Ni-Fe] hydrogenase (H2:NAD oxidoreductase) (HoxU). Its motif for the [4Fe-4S] cluster is G-x-H-x-C-x(2)-C-x(5)-C.

The profile we developed covers the entire His(Cys)3-ligated-type [4Fe-4S] domain.

Last update:

July 2017 / First entry.

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Technical section

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

4FE4S_HC3, PS51839; His(Cys)3-ligated-type [4Fe-4S] domain profile  (MATRIX)


References

1AuthorsOh J.-I. Bowien B.
TitleStructural analysis of the fds operon encoding the NAD+-linked formate dehydrogenase of Ralstonia eutropha.
SourceJ. Biol. Chem. 273:26349-26360(1998).
PubMed ID9756865

2AuthorsPeters J.W. Lanzilotta W.N. Lemon B.J. Seefeldt L.C.
TitleX-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution.
SourceScience 282:1853-1858(1998).
PubMed ID9836629

3AuthorsNicolet Y. Lemon B.J. Fontecilla-Camps J.C. Peters J.W.
TitleA novel FeS cluster in Fe-only hydrogenases.
SourceTrends Biochem. Sci. 25:138-143(2000).
PubMed ID10694885

4AuthorsYano T. Sklar J. Nakamaru-Ogiso E. Takahashi Y. Yagi T. Ohnishi T.
TitleCharacterization of cluster N5 as a fast-relaxing [4Fe-4S] cluster in the Nqo3 subunit of the proton-translocating NADH-ubiquinone oxidoreductase from Paracoccus denitrificans.
SourceJ. Biol. Chem. 278:15514-15522(2003).
PubMed ID12600982
DOI10.1074/jbc.M212275200

5AuthorsSazanov L.A. Hinchliffe P.
TitleStructure of the hydrophilic domain of respiratory complex I from Thermus thermophilus.
SourceScience 311:1430-1436(2006).
PubMed ID16469879
DOI10.1126/science.1123809

6AuthorsNakamaru-Ogiso E. Matsuno-Yagi A. Yoshikawa S. Yagi T. Ohnishi T.
TitleIron-sulfur cluster N5 is coordinated by an HXXXCXXCXXXXXC motif in the NuoG subunit of Escherichia coli NADH:quinone oxidoreductase (complex I).
SourceJ. Biol. Chem. 283:25979-25987(2008).
PubMed ID18603533
DOI10.1074/jbc.M804015200



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