2NUK : Soluble Domain of the Rieske Iron-Sulfur Protein from Rhodobacter sphaeroides

  • Antony R. Crofts (Contributor)
  • Derrick J. Kolling (Contributor)
  • SangMoon Lhee (Contributor)
  • Joseph S. Brunzelle (Contributor)
  • Satish K. Nair (Contributor)

Dataset

Description

Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.2
Classification:OXIDOREDUCTASE
Release Date:2007-04-10
Deposition Date:2006-11-09
Revision Date:2008-05-01#2011-07-13#2017-10-18
Molecular Weight:15337.96
Macromolecule Type:Protein
Residue Count:141
Atom Site Count:1093
DOI:10.2210/pdb2nuk/pdb

Abstract:
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.
Date made available2007
PublisherRCSB-PDB

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