PROSITE logo
Black ribbon
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 PDOC50903
Rubredoxin-like domain profile


View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC50903

Description

The rubredoxin-like domain is a 45- to 55-residue domain containing one iron atom tetrahedrally coordinated to four cysteinyl residues (Fe(S-Cys)4 center). It is involved in electron transfer processes [1,2].

The most conserved feature of the rubredoxin-like domain is the cluster of four cysteines involved in iron binding (Cys-x-x-Cys-x(n)-Cys-x-x-Cys) [2]. Structure analyses of several rubredoxin-like domains have shown that they are folded into a short three-stranded antiparallel β-sheet and a number of loops (see <PDB:1RDG>) [3,4,5,6].

Proteins known to contain a rubredoxin-like domain are listed below:

  • Rubredoxin (Rd), a small electron-transfer prokaryotic protein (see <PDOC00179>).
  • Rubrerythrin (Rr), a non-heme protein isolated from anaerobic sulfate- reducing bacteria.
  • Flavorubredoxin, a bacterial protein involved in elctron transfer processes.
  • Nigerythrin, a prokaryotic protein of unknown function.

The profile we developed covers the entire rubredoxin-like domain.

Last update:

March 2003 / First entry.

-------------------------------------------------------------------------------


Technical section

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

RUBREDOXIN_LIKE, PS50903; Rubredoxin-like domain profile  (MATRIX)


References

1Authorsvan Beeumen J.J. van Driessche G. Liu M.-Y. LeGall J.
SourceJ. Biol. Chem. 266:20645-20653(1991).

2AuthorsPrickril B.C. Kurtz D.M. Jr. LeGall J. Voordouw G.
TitleCloning and sequencing of the gene for rubrerythrin from Desulfovibrio vulgaris (Hildenborough).
SourceBiochemistry 30:11118-11123(1991).
PubMed ID1932032

3AuthorsFrey M. Sieker L. Payan F. Haser R. Bruschi M. Pepe G. LeGall J.
TitleRubredoxin from Desulfovibrio gigas. A molecular model of the oxidized form at 1.4 A resolution.
SourceJ. Mol. Biol. 197:525-541(1987).
PubMed ID3441010

4AuthorsDay M.W. Hsu B.T. Joshua-Tor L. Park J.-B. Zhou Z.H. Adams M.W.W. Rees D.C.
TitleX-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium Pyrococcus furiosus.
SourceProtein Sci. 1:1494-1507(1992).
PubMed ID1303768

5AuthorsSieker L.C. Stenkamp R.E. LeGall J.
TitleRubredoxin in crystalline state.
SourceMethods Enzymol. 243:203-216(1994).
PubMed ID7830611

6AuthorsdeMare F. Kurtz D.M. Jr. Nordlund P.
TitleThe structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains.
SourceNat. Struct. Biol. 3:539-546(1996).
PubMed ID8646540



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.