3D89

Crystal Structure of a Soluble Rieske Ferredoxin from Mus musculus

Summary for 3D89

• Entry DOI: 10.2210/pdb3d89/pdb
• Descriptor: Rieske domain-containing protein, FE2/S2 (INORGANIC) CLUSTER, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: casp target, rieske ferredoxin, [2fe-2s] cluster, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, iron, iron-sulfur, metal-binding, electron transport
• Biological source: Mus musculus (mouse)
• Total number of polymer chains: 1
• Total formula weight: 18189.11

Authors

Levin, E.J.,McCoy, J.G.,Elsen, N.L.,Seder, K.D.,Bingman, C.A.,Wesenberg, G.E.,Fox, B.G.,Phillips Jr., G.N.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2008-05-22, release date: 2008-07-15, Last modification date: 2024-02-21)

Primary citation

Levin, E.J.,Elsen, N.L.,Seder, K.D.,McCoy, J.G.,Fox, B.G.,Phillips, G.N.
X-ray structure of a soluble Rieske-type ferredoxin from Mus musculus.
Acta Crystallogr.,Sect.D, 64:933-940, 2008

PubMed Abstract: The 2.07 A resolution X-ray crystal structure of a soluble Rieske-type ferredoxin from Mus musculus encoded by the gene Mm.266515 is reported. Although they are present as covalent domains in eukaryotic membrane oxidase complexes, soluble Rieske-type ferredoxins have not previously been observed in eukaryotes. The overall structure of the mouse Rieske-type ferredoxin is typical of this class of iron-sulfur proteins and consists of a larger partial beta-barrel domain and a smaller domain containing Cys57, His59, Cys80 and His83 that binds the [2Fe-2S] cluster. The S atoms of the cluster are hydrogen-bonded by six backbone amide N atoms in a pattern typical of membrane-bound high-potential eukaryotic respiratory Rieske ferredoxins. However, phylogenetic analysis suggested that the mouse Rieske-type ferredoxin was more closely related to bacterial Rieske-type ferredoxins. Correspondingly, the structure revealed an extended loop most similar to that seen in Rieske-type ferredoxin subunits of bacterial aromatic dioxygenases, including the positioning of an aromatic side chain (Tyr85) between this loop and the [2Fe-2S] cluster. The mouse Rieske-type ferredoxin was shown to be capable of accepting electrons from both eukaryotic and prokaryotic oxidoreductases, although it was unable to serve as an electron donor for a bacterial monooxygenase complex. The human homolog of mouse Rieske-type ferredoxin was also cloned and purified. It behaved identically to mouse Rieske-type ferredoxin in all biochemical characterizations but did not crystallize. Based on its high sequence identity, the structure of the human homolog is likely to be modeled well by the mouse Rieske-type ferredoxin structure.

PubMed: 18703841
DOI: 10.1107/S0907444908021653

Experimental method

X-RAY DIFFRACTION (2.071 Å)