2nve
From Proteopedia
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| - | [[Image:2nve.jpg|left|200px]] | + | [[Image:2nve.jpg|left|200px]] |
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| - | '''Soluble domain of Rieske Iron Sulfur Protein''' | + | {{Structure |
| + | |PDB= 2nve |SIZE=350|CAPTION= <scene name='initialview01'>2nve</scene>, resolution 1.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= petA, fbcF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]) | ||
| + | }} | ||
| + | |||
| + | '''Soluble domain of Rieske Iron Sulfur Protein''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2NVE is a [ | + | 2NVE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVE OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17223530 17223530] |
[[Category: Rhodobacter sphaeroides]] | [[Category: Rhodobacter sphaeroides]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rieske [2fe-2s] isp]] | [[Category: rieske [2fe-2s] isp]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:51:40 2008'' |
Revision as of 15:51, 20 March 2008
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| , resolution 1.50Å | |||||||
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| Ligands: | and | ||||||
| Gene: | petA, fbcF (Rhodobacter sphaeroides) | ||||||
| Activity: | Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
2NVE is a Single protein structure of sequence from Rhodobacter sphaeroides. 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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