This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2nwf
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2nwf.gif|left|200px]] | + | [[Image:2nwf.gif|left|200px]] |
| - | + | ||
| - | '''Soluble domain of Rieske Iron Sulfur Protein''' | + | {{Structure |
| + | |PDB= 2nwf |SIZE=350|CAPTION= <scene name='initialview01'>2nwf</scene>, resolution 1.10Å | ||
| + | |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== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2NWF is a [ | + | 2NWF 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=2NWF 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]] | ||
| Line 23: | Line 32: | ||
[[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 17:52:03 2008'' |
Revision as of 15:52, 20 March 2008
| |||||||
| , resolution 1.10Å | |||||||
|---|---|---|---|---|---|---|---|
| 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
2NWF 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]]
Page seeded by OCA on Thu Mar 20 17:52:03 2008
