2num: Difference between revisions

Revision as of 19:11, 21 February 2008

Soluble domain of Rieske Iron-Sulfur Protein

OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 18:11:11 2008

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OCA

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-[[Image:2num.jpg|left|200px]]<br /><applet load="2num" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2num.jpg|left|200px]]<br /><applet load="2num" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2num, resolution 1.50&Aring;" />
 '''Soluble domain of Rieske Iron-Sulfur Protein'''<br />
 ==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--&gt;Ala, Ser-154--&gt;Thr, Ser-154--&gt;Cys, Tyr-156--&gt;Phe, and Tyr-156--&gt;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.
+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--&gt;Ala, Ser-154--&gt;Thr, Ser-154--&gt;Cys, Tyr-156--&gt;Phe, and Tyr-156--&gt;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==
-NUM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with FES as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ubiquinol--cytochrome-c_reductase Ubiquinol--cytochrome-c reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.2.2 1.10.2.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NUM OCA].
+NUM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ubiquinol--cytochrome-c_reductase Ubiquinol--cytochrome-c reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.2.2 1.10.2.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NUM OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Ubiquinol--cytochrome-c reductase]]
 [[Category: Brunzelle, J.]]
-[[Category: Crofts, A.R.]]
+[[Category: Crofts, A R.]]
 [[Category: Kolling, D.]]
 [[Category: Lhee, S.]]
-[[Category: Nair, S.K.]]
+[[Category: Nair, S K.]]
 [[Category: FES]]
 [[Category: iron sulfur cluster]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:55:24 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:11 2008''