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| | <StructureSection load='4h0k' size='340' side='right'caption='[[4h0k]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='4h0k' size='340' side='right'caption='[[4h0k]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4h0k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H0K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H0K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4h0k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H0K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gyd|4gyd]], [[4h0j|4h0j]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">petJ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=103690 Anabaena 7120])</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=4h0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h0k OCA], [https://pdbe.org/4h0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h0k RCSB], [https://www.ebi.ac.uk/pdbsum/4h0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h0k ProSAT]</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=4h0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h0k OCA], [http://pdbe.org/4h0k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h0k RCSB], [http://www.ebi.ac.uk/pdbsum/4h0k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h0k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CYC6_NOSS1 CYC6_NOSS1]] Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis (By similarity). | + | [https://www.uniprot.org/uniprot/CYC6_NOSS1 CYC6_NOSS1] Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | + | *[[Cytochrome f 3D structures|Cytochrome f 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anabaena 7120]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cavazzini, D]] | + | [[Category: Nostoc sp. PCC 7120 = FACHB-418]] |
| - | [[Category: Pannu, N S]] | + | [[Category: Cavazzini D]] |
| - | [[Category: Rossi, G L]] | + | [[Category: Pannu NS]] |
| - | [[Category: Skubak, P]] | + | [[Category: Rossi GL]] |
| - | [[Category: Ubbink, M]] | + | [[Category: Skubak P]] |
| - | [[Category: Electron transport]]
| + | [[Category: Ubbink M]] |
| - | [[Category: Heme binding]]
| + | |
| Structural highlights
Function
CYC6_NOSS1 Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis (By similarity).
Publication Abstract from PubMed
The rapid transfer of electrons in the photosynthetic redox chain is achieved by the formation of short-lived complexes of cytochrome b6f with the electron transfer proteins plastocyanin and cytochrome c6. A balance must exist between fast intermolecular electron transfer and rapid dissociation, which requires the formation of a complex that has limited specificity. The interaction of the soluble fragment of cytochrome f and cytochrome c6 from the cyanobacterium Nostoc sp. PCC 7119 was studied using NMR spectroscopy and X-ray diffraction. The crystal structures of wild type, M58H and M58C cytochrome c6 were determined. The M58C variant is an excellent low potential mimic of the wild type protein and was used in chemical shift perturbation and paramagnetic relaxation NMR experiments to characterize the complex with cytochrome f. The interaction is highly dynamic and can be described as a pure encounter complex, with no dominant stereospecific complex. Ensemble docking calculations and Monte-Carlo simulations suggest a model in which charge-charge interactions pre-orient cytochrome c6 with its haem edge toward cytochrome f to form an ensemble of orientations with extensive contacts between the hydrophobic patches on both cytochromes, bringing the two haem groups sufficiently close to allow for rapid electron transfer. This model of complex formation allows for a gradual increase and decrease of the hydrophobic interactions during association and dissociation, thus avoiding a high transition state barrier that would slow down the dissociation process.
The dynamic complex of cytochrome c6 and cytochrome f studied with paramagnetic NMR spectroscopy.,Diaz-Moreno I, Hulsker R, Skubak P, Foerster JM, Cavazzini D, Finiguerra MG, Diaz-Quintana A, Moreno-Beltran B, Rossi GL, Ullmann GM, Pannu NS, De la Rosa MA, Ubbink M Biochim Biophys Acta. 2014 Aug;1837(8):1305-15. doi:, 10.1016/j.bbabio.2014.03.009. Epub 2014 Mar 28. PMID:24685428[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Diaz-Moreno I, Hulsker R, Skubak P, Foerster JM, Cavazzini D, Finiguerra MG, Diaz-Quintana A, Moreno-Beltran B, Rossi GL, Ullmann GM, Pannu NS, De la Rosa MA, Ubbink M. The dynamic complex of cytochrome c6 and cytochrome f studied with paramagnetic NMR spectroscopy. Biochim Biophys Acta. 2014 Aug;1837(8):1305-15. doi:, 10.1016/j.bbabio.2014.03.009. Epub 2014 Mar 28. PMID:24685428 doi:http://dx.doi.org/10.1016/j.bbabio.2014.03.009
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