2NVF
Soluble domain of Rieske Iron-Sulfur protein.
Summary for 2NVF
| Entry DOI | 10.2210/pdb2nvf/pdb |
| Related | 2NUK 2NUM 2NVE 2NVG 2NWF |
| Descriptor | Ubiquinol-cytochrome c reductase iron-sulfur subunit, FE2/S2 (INORGANIC) CLUSTER, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | rieske [2fe-2s] protein, oxidoreductase |
| Biological source | Rhodobacter sphaeroides |
| Cellular location | Cell membrane; Single-pass membrane protein: Q02762 |
| Total number of polymer chains | 1 |
| Total formula weight | 15538.21 |
| Authors | Kolling, D.,Brunzelle, J.,Lhee, S.,Crofts, A.R.,Nair, S.K. (deposition date: 2006-11-12, release date: 2007-02-06, Last modification date: 2024-10-09) |
| Primary citation | Kolling, D.J.,Brunzelle, J.S.,Lhee, S.,Crofts, A.R.,Nair, S.K. Atomic resolution structures of rieske iron-sulfur protein: role of hydrogen bonds in tuning the redox potential of iron-sulfur clusters. Structure, 15:29-38, 2007 Cited by PubMed Abstract: 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. PubMed: 17223530DOI: 10.1016/j.str.2006.11.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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