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| | <StructureSection load='2fwl' size='340' side='right'caption='[[2fwl]], [[NMR_Ensembles_of_Models | 3 NMR models]]' scene=''> | | <StructureSection load='2fwl' size='340' side='right'caption='[[2fwl]], [[NMR_Ensembles_of_Models | 3 NMR models]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2fwl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FWL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FWL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2fwl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet8 Thet8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FWL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ehk|1ehk]], [[1dt1|1dt1]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ehk|1ehk]], [[1dt1|1dt1]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fwl OCA], [http://pdbe.org/2fwl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fwl RCSB], [http://www.ebi.ac.uk/pdbsum/2fwl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fwl ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fwl OCA], [https://pdbe.org/2fwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fwl RCSB], [https://www.ebi.ac.uk/pdbsum/2fwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fwl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CY552_THETH CY552_THETH]] This monoheme basic protein appears to function as an electron donor to cytochrome oxidase in T.thermophilus. [[http://www.uniprot.org/uniprot/COX2_THETH COX2_THETH]] Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | + | [[https://www.uniprot.org/uniprot/CY552_THETH CY552_THETH]] This monoheme basic protein appears to function as an electron donor to cytochrome oxidase in T.thermophilus. [[https://www.uniprot.org/uniprot/COX2_THETH COX2_THETH]] Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| | + | *[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]] |
| | *[[Cytochrome c oxidase 3D structures|Cytochrome c oxidase 3D structures]] | | *[[Cytochrome c oxidase 3D structures|Cytochrome c oxidase 3D structures]] |
| - | *[[Nitrite reductase 3D structures|Nitrite reductase 3D structures]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Structural highlights
Function
[CY552_THETH] This monoheme basic protein appears to function as an electron donor to cytochrome oxidase in T.thermophilus. [COX2_THETH] Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Muresanu L, Pristovsek P, Lohr F, Maneg O, Mukrasch MD, Ruterjans H, Ludwig B, Lucke C. The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase. A combined NMR and computational approach. J Biol Chem. 2006 May 19;281(20):14503-13. Epub 2006 Mar 22. PMID:16554303 doi:10.1074/jbc.M601108200
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