Protein Family Models

This family is the catalytic domain of aromatic-ring- hydroxylating dioxygenase systems. The active site contains a non-heme ferrous ion coordinated by three ligands. (from Pfam)

Date:

2024-12-02

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

aromatic ring-hydroxylating oxygenase subunit alpha is the catalytic component of a complex that catalyzes the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds

Date:

2024-11-20