Protein Family Models

The rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion, while the other Fe ion is coordinated by two conserved histidines. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in this motif form a disulphide bridge, which stabilises the protein [4]. [1]. 8736555. Structure 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. Iwata S, Saynovits M, Link TA, Michel H. Structure 1996;4:567-579. [2]. 1961737. Functional analysis in yeast of cDNA coding for the mitochondrial Rieske iron-sulfur protein of higher plants. Huang JT, Struck F, Matzinger DF, Levings CS;. Proc Natl Acad Sci U S A 1991;88:10716-10720. [3]. 8386158. The mitochondrial targeting presequence of the Rieske iron-sulfur protein is processed in a single step after insertion into the cytochrome bc1 complex in mammals and retained as a subunit in the complex. Brandt U, Yu L, Yu CA, Trumpower BL;. J Biol Chem 1993;268:8387-8390. [4]. 19862563. Role of a novel disulfide bridge within the all-beta fold of soluble Rieske proteins. Botelho HM, Leal SS, Veith A, Prosinecki V, Bauer C, Frohlich R, Kletzin A, Gomes CM;. J Biol Inorg Chem. 2010;15:271-281. (from Pfam)

Date:

2024-10-16

Rieske (2Fe-2S) protein contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs, similar to Streptomyces cytochrome bc1 complex Rieske iron-sulfur subunit, an essential component of the respiratory electron transport chain required for ATP synthesis.

Date:

2022-07-26