Structural highlights
Function
[RUBR_CLOPA] Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Five different metal-substituted forms of Clostridium pasteurianum rubredoxin have been prepared and crystallized. The single Fe atom present in the Fe(S-Cys)(4) site of the native form of the protein was exchanged in turn for Co, Ni, Ga, Cd and Hg. All five forms of rubredoxin crystallized in space group R3 and were isomorphous with the native protein. The Co-, Ni- and Ga-substituted proteins exhibited metal sites with geometries similar to that of the Fe form (effective D(2d) local symmetry), as did the Cd and Hg proteins, but with a significant expansion of the metal-sulfur bond lengths. A knowledge of these structures contributes to a molecular understanding of the function of this simple iron-sulfur electron-transport protein.
Metal-substituted derivatives of the rubredoxin from Clostridium pasteurianum.,Maher M, Cross M, Wilce MC, Guss JM, Wedd AG Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):298-303. Epub 2004, Jan 23. PMID:14747706[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Maher M, Cross M, Wilce MC, Guss JM, Wedd AG. Metal-substituted derivatives of the rubredoxin from Clostridium pasteurianum. Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):298-303. Epub 2004, Jan 23. PMID:14747706 doi:10.1107/S090744490302794X
