2nvg

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[[Image:2nvg.jpg|left|200px]]
[[Image:2nvg.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2nvg |SIZE=350|CAPTION= <scene name='initialview01'>2nvg</scene>, resolution 1.35&Aring;
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The line below this paragraph, containing "STRUCTURE_2nvg", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquinol--cytochrome-c_reductase Ubiquinol--cytochrome-c reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.2.2 1.10.2.2] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= petA, fbcF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides])
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-->
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|DOMAIN=
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{{STRUCTURE_2nvg| PDB=2nvg | SCENE= }}
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|RELATEDENTRY=[[2nuk|2NUK]], [[2num|2NUM]], [[2nve|2NVE]], [[2nvf|2NVF]], [[2nwf|2NWF]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nvg OCA], [http://www.ebi.ac.uk/pdbsum/2nvg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nvg RCSB]</span>
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}}
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'''Soluble domain of Rieske Iron Sulfur protein.'''
'''Soluble domain of Rieske Iron Sulfur protein.'''
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[[Category: Lhee, S.]]
[[Category: Lhee, S.]]
[[Category: Nair, S K.]]
[[Category: Nair, S K.]]
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[[Category: rieske [2fe-2s] protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:57:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:08:57 2008''
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Revision as of 06:57, 4 May 2008

Image:2nvg.jpg

Template:STRUCTURE 2nvg

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

2NVG 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 09:57:33 2008

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