2nvf: Difference between revisions

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[[Image:2nvf.jpg|left|200px]]<br /><applet load="2nvf" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2nvf.jpg|left|200px]]
caption="2nvf, resolution 1.50&Aring;" />
 
'''Soluble domain of Rieske Iron-Sulfur protein.'''<br />
{{Structure
|PDB= 2nvf |SIZE=350|CAPTION= <scene name='initialview01'>2nvf</scene>, resolution 1.50&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|ACTIVITY= [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]
|GENE= petA, fbcF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides])
}}
 
'''Soluble domain of Rieske Iron-Sulfur protein.'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2NVF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=FES:'>FES</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVF OCA].  
2NVF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVF OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17223530 17223530]
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:[http://www.ncbi.nlm.nih.gov/pubmed/17223530 17223530]
[[Category: Rhodobacter sphaeroides]]
[[Category: Rhodobacter sphaeroides]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: rieske [2fe-2s] protein]]
[[Category: rieske [2fe-2s] protein]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:32 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:51:39 2008''

Revision as of 18:51, 20 March 2008

File:2nvf.jpg


PDB ID 2nvf

Drag the structure with the mouse to rotate
, resolution 1.50Å
Ligands: and
Gene: petA, fbcF (Rhodobacter sphaeroides)
Activity: Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2
Coordinates: save as pdb, mmCIF, xml



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

2NVF 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 [[Category: rieske [2fe-2s] protein]]

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