PDBsum entry 3d89

Electron transport

PDB id: 3d89

Contents

Protein chain

136 a.a. *

Ligands

FES

EDO

Waters ×48

* Residue conservation analysis

PDB id:

3d89

Name:

Electron transport

Title:

Crystal structure of a soluble rieske ferredoxin from mus musculus

Structure:

Rieske domain-containing protein. Chain: a. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: rfesd. Expressed in: escherichia coli.

Resolution:

2.07Å R-factor: 0.200 R-free: 0.228

Authors:

E.J.Levin,J.G.Mccoy,N.L.Elsen,K.D.Seder,C.A.Bingman,G.E.Wesenberg, B.G.Fox,G.N.Phillips Jr.,Center For Eukaryotic Structural Genomics (Cesg)

Key ref:

E.J.Levin et al. (2008). X-ray structure of a soluble Rieske-type ferredoxin from Mus musculus. Acta Crystallogr D Biol Crystallogr, 64, 933-940. PubMed id: 18703841 DOI: 10.1107/S0907444908021653

Date:

22-May-08 Release date: 15-Jul-08

Protein chain

Q8K2P6  (RFESD_MOUSE) -  Rieske domain-containing protein from Mus musculus

Seq: 157 a.a.

Struc: 136 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1107/S0907444908021653

Acta Crystallogr D Biol Crystallogr 64:933-940 (2008)

PubMed id: 18703841

X-ray structure of a soluble Rieske-type ferredoxin from Mus musculus.

E.J.Levin, N.L.Elsen, K.D.Seder, J.G.McCoy, B.G.Fox, G.N.Phillips.

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.

Selected figure(s)

Figure 3.
Figure 3 Ribbon representation of mouse soluble Rieske ferredoxin. The large domain is shown in blue and the cluster-binding domain in green. The iron-sulfur cluster is shown as spheres, with the S atoms colored yellow and the Fe atoms gray. The dashed line indicates the approximate location of five disordered residues in the 8- X loop.

Figure 5.
Figure 5 Comparison of Rieske ferredoxin folds and the MRF active site. (a) Stereo image of the alignment of MRF (cyan), BphF (PDB code 1fqt , gray), T4moC (PDB code 1vm9 , green) and CarAc (PDB code 1vck , red). The positioning of the space-filling representation of the iron-sulfur cluster corresponds to its location in the MRF structure. (b) Stereo image of the MRF active site and residues participating in hydrogen bonding to the atoms of the iron-sulfur cluster and the cysteine S atoms, which are represented as spheres.

The above figures are reprinted from an Open Access publication published by the IUCr: Acta Crystallogr D Biol Crystallogr (2008, 64, 933-940) copyright 2008.

Figures were selected by an automated process.