2nwf: Difference between revisions

Revision as of 09:59, 4 May 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

2NWF is a Single protein structure of sequence from Rhodobacter sphaeroides. 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 Sun May 4 09:59:41 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 [[Image:2nwf.gif|left|200px]]
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-}}
 '''Soluble domain of Rieske Iron Sulfur Protein'''
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 [[Category: Lhee, S.]]
 [[Category: Nair, S K.]]
-[[Category: rieske [2fe-2s] isp]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 09:59:41 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:09:22 2008''