2nwf: Difference between revisions

Revision as of 14:35, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2nwf.png

Template:STRUCTURE 2nwf

Soluble domain of Rieske Iron Sulfur ProteinSoluble domain of Rieske Iron Sulfur Protein

Template:ABSTRACT PUBMED 17223530

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 Mon Jul 28 14:35:49 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2nwf.gif|left|200px]]
+{{Seed}}
+[[Image:2nwf.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2nwf|  PDB=2nwf  |  SCENE=  }}
-'''Soluble domain of Rieske Iron Sulfur Protein'''
+===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--&gt;Ala, Ser-154--&gt;Thr, Ser-154--&gt;Cys, Tyr-156--&gt;Phe, and Tyr-156--&gt;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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17223530}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17223530 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17223530}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Lhee, S.]]
 [[Category: Nair, S K.]]
-''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 Jul 28 14:35:49 2008''