2nvg
From Proteopedia
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|PDB= 2nvg |SIZE=350|CAPTION= <scene name='initialview01'>2nvg</scene>, resolution 1.35Å | |PDB= 2nvg |SIZE=350|CAPTION= <scene name='initialview01'>2nvg</scene>, resolution 1.35Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene> | + | |LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <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] | + | |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> |
|GENE= petA, fbcF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]) | |GENE= petA, fbcF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2nuk|2NUK]], [[2num|2NUM]], [[2nve|2NVE]], [[2nvf|2NVF]], [[2nwf|2NWF]] | ||
| + | |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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[[Category: Lhee, S.]] | [[Category: Lhee, S.]] | ||
[[Category: Nair, S K.]] | [[Category: Nair, S K.]] | ||
| - | [[Category: FES]] | ||
| - | [[Category: GOL]] | ||
[[Category: rieske [2fe-2s] protein]] | [[Category: rieske [2fe-2s] protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:08:57 2008'' |
Revision as of 01:08, 31 March 2008
| |||||||
| , resolution 1.35Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | petA, fbcF (Rhodobacter sphaeroides) | ||||||
| Activity: | Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2 | ||||||
| Related: | 2NUK, 2NUM, 2NVE, 2NVF, 2NWF
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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[[Category: rieske [2fe-2s] protein]]
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