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.
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.
PROSITE documentation PDOC51839His(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:
References
| 1 | Authors | Oh J.-I. Bowien B. |
| Title | Structural analysis of the fds operon encoding the NAD+-linked formate dehydrogenase of Ralstonia eutropha. | |
| Source | J. Biol. Chem. 273:26349-26360(1998). | |
| PubMed ID | 9756865 |
| 2 | Authors | Peters J.W. Lanzilotta W.N. Lemon B.J. Seefeldt L.C. |
| Title | X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution. | |
| Source | Science 282:1853-1858(1998). | |
| PubMed ID | 9836629 |
| 3 | Authors | Nicolet Y. Lemon B.J. Fontecilla-Camps J.C. Peters J.W. |
| Title | A novel FeS cluster in Fe-only hydrogenases. | |
| Source | Trends Biochem. Sci. 25:138-143(2000). | |
| PubMed ID | 10694885 |
| 4 | Authors | Yano T. Sklar J. Nakamaru-Ogiso E. Takahashi Y. Yagi T. Ohnishi T. |
| Title | Characterization of cluster N5 as a fast-relaxing [4Fe-4S] cluster in the Nqo3 subunit of the proton-translocating NADH-ubiquinone oxidoreductase from Paracoccus denitrificans. | |
| Source | J. Biol. Chem. 278:15514-15522(2003). | |
| PubMed ID | 12600982 | |
| DOI | 10.1074/jbc.M212275200 |
| 5 | Authors | Sazanov L.A. Hinchliffe P. |
| Title | Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. | |
| Source | Science 311:1430-1436(2006). | |
| PubMed ID | 16469879 | |
| DOI | 10.1126/science.1123809 |
| 6 | Authors | Nakamaru-Ogiso E. Matsuno-Yagi A. Yoshikawa S. Yagi T. Ohnishi T. |
| Title | Iron-sulfur cluster N5 is coordinated by an HXXXCXXCXXXXXC motif in the NuoG subunit of Escherichia coli NADH:quinone oxidoreductase (complex I). | |
| Source | J. Biol. Chem. 283:25979-25987(2008). | |
| PubMed ID | 18603533 | |
| DOI | 10.1074/jbc.M804015200 |
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