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.
2nvf
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2nvf.jpg|left|200px]] | [[Image:2nvf.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2nvf", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_2nvf| PDB=2nvf | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Soluble domain of Rieske Iron-Sulfur protein.''' | '''Soluble domain of Rieske Iron-Sulfur protein.''' | ||
| Line 31: | Line 28: | ||
[[Category: Lhee, S.]] | [[Category: Lhee, S.]] | ||
[[Category: Nair, S K.]] | [[Category: Nair, S K.]] | ||
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:57:26 2008'' | |
| - | + | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:57, 4 May 2008
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
2NVF 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 Page seeded by OCA on Sun May 4 09:57:26 2008
