2nvg
From Proteopedia
(New page: 200px<br /><applet load="2nvg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nvg, resolution 1.35Å" /> '''Soluble domain of Ri...) |
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| - | [[Image:2nvg.jpg|left|200px]]<br /><applet load="2nvg" size=" | + | [[Image:2nvg.jpg|left|200px]]<br /><applet load="2nvg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2nvg, resolution 1.35Å" /> | caption="2nvg, resolution 1.35Å" /> | ||
'''Soluble domain of Rieske Iron Sulfur protein.'''<br /> | '''Soluble domain of Rieske Iron Sulfur protein.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Rieske [2Fe-2S] iron-sulfur protein of cytochrome bc(1) functions as | + | 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== | ==About this Structure== | ||
| - | 2NVG 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 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 2NVG 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> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=2NVG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ubiquinol--cytochrome-c reductase]] | [[Category: Ubiquinol--cytochrome-c reductase]] | ||
[[Category: Brunzelle, J.]] | [[Category: Brunzelle, J.]] | ||
| - | [[Category: Crofts, A | + | [[Category: Crofts, A R.]] |
[[Category: Kolling, D.]] | [[Category: Kolling, D.]] | ||
[[Category: Lhee, S.]] | [[Category: Lhee, S.]] | ||
| - | [[Category: Nair, S | + | [[Category: Nair, S K.]] |
[[Category: FES]] | [[Category: FES]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: rieske [2fe-2s] protein]] | [[Category: rieske [2fe-2s] protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:35 2008'' |
Revision as of 16:11, 21 February 2008
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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
2NVG is a Single protein structure of sequence from Rhodobacter sphaeroides with and 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] protein]]
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