Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.1
Classification:OXIDOREDUCTASE
Release Date:2007-04-10
Deposition Date:2006-11-14
Revision Date:2008-05-01#2011-07-13
Molecular Weight:15637.28
Macromolecule Type:Protein
Residue Count:141
Atom Site Count:1145
DOI:10.2210/pdb2nwf/pdb
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.
Resolution:1.1
Classification:OXIDOREDUCTASE
Release Date:2007-04-10
Deposition Date:2006-11-14
Revision Date:2008-05-01#2011-07-13
Molecular Weight:15637.28
Macromolecule Type:Protein
Residue Count:141
Atom Site Count:1145
DOI:10.2210/pdb2nwf/pdb
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.
| Date made available | 2007 |
|---|---|
| Publisher | RCSB-PDB |