1rie: Difference between revisions
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[[Image:1rie.gif|left|200px]] | [[Image:1rie.gif|left|200px]] | ||
'''STRUCTURE OF A WATER SOLUBLE FRAGMENT OF THE RIESKE IRON-SULFUR PROTEIN OF THE BOVINE HEART MITOCHONDRIAL CYTOCHROME BC1-COMPLEX''' | {{Structure | ||
|PDB= 1rie |SIZE=350|CAPTION= <scene name='initialview01'>1rie</scene>, resolution 1.5Å | |||
|SITE= <scene name='pdbsite=IRO:Fe2/S2+Site'>IRO</scene> | |||
|LIGAND= <scene name='pdbligand=FES:FE2/S2 (INORGANIC) CLUSTER'>FES</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= | |||
}} | |||
'''STRUCTURE OF A WATER SOLUBLE FRAGMENT OF THE RIESKE IRON-SULFUR PROTEIN OF THE BOVINE HEART MITOCHONDRIAL CYTOCHROME BC1-COMPLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1RIE is a [ | 1RIE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RIE OCA]. | ||
==Reference== | ==Reference== | ||
Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 A resolution., Iwata S, Saynovits M, Link TA, Michel H, Structure. 1996 May 15;4(5):567-79. PMID:[http:// | Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 A resolution., Iwata S, Saynovits M, Link TA, Michel H, Structure. 1996 May 15;4(5):567-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8736555 8736555] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cytochrome bc1 complex]] | [[Category: cytochrome bc1 complex]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
[[Category: histidine | [[Category: histidine ligand]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: rieske iron-sulfur cluster]] | [[Category: rieske iron-sulfur cluster]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:52:01 2008'' | ||
Revision as of 11:52, 20 March 2008
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| 1rie, resolution 1.5Å | |||||||||||||
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| Sites: | IRO | ||||||||||||
| Ligands: | FES | ||||||||||||
| Activity: | Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
STRUCTURE OF A WATER SOLUBLE FRAGMENT OF THE RIESKE IRON-SULFUR PROTEIN OF THE BOVINE HEART MITOCHONDRIAL CYTOCHROME BC1-COMPLEX
Overview
BACKGROUND: The 'Rieske' iron-sulfur protein is the primary electron acceptor during hydroquinone oxidation in cytochrome bc complexes. The spectroscopic and electrochemical properties of the 'Rieske' [2Fe-2S] cluster differ significantly from those of other iron-sulfur clusters. A 129-residue water soluble fragment containing the intact [2Fe-2S] cluster was isolated following proteolytic digestion of the bc1 complex and used for structural studies. RESULTS: The structure of the Rieske iron-sulfur fragment containing the reduced [2Fe-2S] cluster has been determined using the multiwavelength anomalous diffraction (MAD) technique and refined at 1.5 A resolution. The fragment has a novel overall fold that includes three sheets of beta strands. The iron atoms of the [2Fe-2S] cluster are coordinated by two cysteine (Fe-1) and two histidine (Fe-2) residues, respectively, with the histidine ligands completely exposed to the solvent. This is in contrast to the four cysteine coordination pattern observed in previously characterised [2Fe-2S] ferredoxins. The cluster-binding fold is formed by two loops connected by a disulfide bridge; these loops superpose with the metal-binding loops of rubredoxins. The environment of the cluster is stabilised by an extensive hydrogen-bond network. CONCLUSIONS: The high-resolution structure supports the proposed coordination pattern involving histidine ligands and provides a basis for a detailed analysis of the spectroscopic and electrochemical properties. As the cluster is located at the tip of the protein, it might come into close contact with cytochrome b. The exposed N epsilon atoms of the histidine ligands of the cluster are readily accessible to quinones and inhibitors within the hydroquinone oxidation (QP) pocket of the bc1 complex and may undergo redox-dependent protonation/deprotonation.
About this Structure
1RIE is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 A resolution., Iwata S, Saynovits M, Link TA, Michel H, Structure. 1996 May 15;4(5):567-79. PMID:8736555
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