2fwl
From Proteopedia
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| - | [[Image:2fwl.gif|left|200px]]< | + | [[Image:2fwl.gif|left|200px]] |
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| - | '''The cytochrome c552/CuA complex from Thermus thermophilus''' | + | {{Structure |
| + | |PDB= 2fwl |SIZE=350|CAPTION= <scene name='initialview01'>2fwl</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HEC:HEME+C'>HEC</scene> and <scene name='pdbligand=CUA:DINUCLEAR COPPER ION'>CUA</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''The cytochrome c552/CuA complex from Thermus thermophilus''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FWL is a [ | + | 2FWL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FWL OCA]. |
==Reference== | ==Reference== | ||
| - | The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase. A combined NMR and computational approach., Muresanu L, Pristovsek P, Lohr F, Maneg O, Mukrasch MD, Ruterjans H, Ludwig B, Lucke C, J Biol Chem. 2006 May 19;281(20):14503-13. Epub 2006 Mar 22. PMID:[http:// | + | The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase. A combined NMR and computational approach., Muresanu L, Pristovsek P, Lohr F, Maneg O, Mukrasch MD, Ruterjans H, Ludwig B, Lucke C, J Biol Chem. 2006 May 19;281(20):14503-13. Epub 2006 Mar 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16554303 16554303] |
[[Category: Cytochrome-c oxidase]] | [[Category: Cytochrome-c oxidase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: CUA]] | [[Category: CUA]] | ||
[[Category: HEC]] | [[Category: HEC]] | ||
| - | [[Category: docking | + | [[Category: docking calculation]] |
[[Category: electron transfer pathway]] | [[Category: electron transfer pathway]] | ||
[[Category: redox protein complex]] | [[Category: redox protein complex]] | ||
| - | ''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 16:57:37 2008'' |
Revision as of 14:57, 20 March 2008
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| Ligands: | and | ||||||
| Activity: | Cytochrome-c oxidase, with EC number 1.9.3.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The cytochrome c552/CuA complex from Thermus thermophilus
Overview
The structural analysis of the redox complex between the soluble cytochrome c552 and the membrane-integral cytochrome ba3 oxidase of Thermus thermophilus is complicated by the transient nature of this protein-protein interaction. Using NMR-based chemical shift perturbation mapping, however, we identified the contact regions between cytochrome c552 and the CuA domain, the fully functional water-soluble fragment of subunit II of the ba3 oxidase. First we determined the complete backbone resonance assignments of both proteins for each redox state. Subsequently, two-dimensional [15N,1H]TROSY spectra recorded for each redox partner both in free and complexed state indicated those surface residues affected by complex formation between the two proteins. This chemical shift analysis performed for both redox states provided a topological description of the contact surface on each partner molecule. Remarkably, very pronounced indirect effects, which were observed on the back side of the heme cleft only in the reduced state, suggested that alterations of the electron distribution in the porphyrin ring due to formation of the protein-protein complex are apparently sensed even beyond the heme propionate groups. The contact residues of each redox partner, as derived from the chemical shift perturbation mapping, were employed for a protein-protein docking calculation that provided a structure ensemble of 10 closely related conformers representing the complex between cytochrome c552 and the CuA domain. Based on these structures, the electron transfer pathway from the heme of cytochrome c552 to the CuA center of the ba3 oxidase has been predicted.
About this Structure
2FWL is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase. A combined NMR and computational approach., Muresanu L, Pristovsek P, Lohr F, Maneg O, Mukrasch MD, Ruterjans H, Ludwig B, Lucke C, J Biol Chem. 2006 May 19;281(20):14503-13. Epub 2006 Mar 22. PMID:16554303
Page seeded by OCA on Thu Mar 20 16:57:37 2008
