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spinqualitylabelsall models 2nwf, resolution 1.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Soluble domain of Rieske Iron Sulfur Protein

Overview

The Rieske [2Fe-2S] iron-sulfur protein of cytochrome bc(1) functions as, the initial electron acceptor in the rate-limiting step of the catalytic, reaction. Prior studies have established roles for a number of conserved, residues that hydrogen bond to ligands of the [2Fe-2S] cluster. We have, constructed site-specific variants at two of these residues, measured, their thermodynamic and functional properties, and determined atomic, resolution X-ray crystal structures for the native protein at 1.2 A, resolution and for five variants (Ser-154-->Ala, Ser-154-->Thr, Ser-154-->Cys, Tyr-156-->Phe, and Tyr-156-->Trp) to resolutions between, 1.5 A and 1.1 A. These structures and complementary biophysical data, provide a molecular framework for understanding the role hydrogen bonds to, the cluster play in tuning thermodynamic properties, and hence the rate of, this bioenergetic reaction. These studies provide a detailed, structure-function dissection of the role of hydrogen bonds in tuning the, redox potentials of [2Fe-2S] clusters.

About this Structure

2NWF is a Single protein structure of sequence from Rhodobacter sphaeroides with FES and GOL as ligands. Active as Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2 Full crystallographic information is available from OCA.

Reference

Atomic resolution structures of rieske iron-sulfur protein: role of hydrogen bonds in tuning the redox potential of iron-sulfur clusters., Kolling DJ, Brunzelle JS, Lhee S, Crofts AR, Nair SK, Structure. 2007 Jan;15(1):29-38. PMID:17223530[[Category: rieske [2fe-2s] isp]]

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