2nve

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{{STRUCTURE_2nve| PDB=2nve | SCENE= }}
{{STRUCTURE_2nve| PDB=2nve | SCENE= }}
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'''Soluble domain of Rieske Iron Sulfur Protein'''
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===Soluble domain of Rieske Iron Sulfur Protein===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17223530 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17223530}}
==About this Structure==
==About this Structure==
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[[Category: Lhee, S.]]
[[Category: Lhee, S.]]
[[Category: Nair, S K.]]
[[Category: Nair, S K.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:57:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:22:38 2008''

Revision as of 06:22, 29 July 2008

Image:2nve.png

Template:STRUCTURE 2nve

Soluble domain of Rieske Iron Sulfur Protein

Template:ABSTRACT PUBMED 17223530

About this Structure

2NVE 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

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