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| ==Crystal structure of cytochrome c552 from Thermus thermophilus at pH 5.44== | | ==Crystal structure of cytochrome c552 from Thermus thermophilus at pH 5.44== |
- | <StructureSection load='3vnw' size='340' side='right' caption='[[3vnw]], [[Resolution|resolution]] 1.97Å' scene=''> | + | <StructureSection load='3vnw' size='340' side='right'caption='[[3vnw]], [[Resolution|resolution]] 1.97Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3vnw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VNW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VNW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vnw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VNW FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 1.97Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cycA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=3vnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vnw OCA], [http://pdbe.org/3vnw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vnw RCSB], [http://www.ebi.ac.uk/pdbsum/3vnw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vnw 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=3vnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vnw OCA], [https://pdbe.org/3vnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vnw RCSB], [https://www.ebi.ac.uk/pdbsum/3vnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vnw 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. | + | [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. |
| <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== |
- | *[[Nitric reductase|Nitric reductase]] | + | *[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Flavobacterium thermophilum yoshida and oshima 1971]] | + | [[Category: Large Structures]] |
- | [[Category: Bouley-Ford, N D]] | + | [[Category: Thermus thermophilus]] |
- | [[Category: Gray, H B]] | + | [[Category: Bouley-Ford ND]] |
- | [[Category: Keller, G E]] | + | [[Category: Gray HB]] |
- | [[Category: Winkler, J R]] | + | [[Category: Keller GE]] |
- | [[Category: Yamada, S]] | + | [[Category: Winkler JR]] |
- | [[Category: Cytochrome c]]
| + | [[Category: Yamada S]] |
- | [[Category: Electron transfer]]
| + | |
- | [[Category: Electron transport]]
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| Structural highlights
Function
CY552_THETH This monoheme basic protein appears to function as an electron donor to cytochrome oxidase in T.thermophilus.
Publication Abstract from PubMed
We have investigated the folding dynamics of Thermus thermophilus cytochrome c(552) by time-resolved fluorescence energy transfer between the heme and each of seven site-specific fluorescent probes. We have found both an equilibrium unfolding intermediate and a distinct refolding intermediate from kinetics studies. Depending on the protein region monitored, we observed either two-state or three-state denaturation transitions. The unfolding intermediate associated with three-state folding exhibited native contacts in beta-sheet and C-terminal helix regions. We probed the formation of a refolding intermediate by time-resolved fluorescence energy transfer between residue 110 and the heme using a continuous flow mixer. The intermediate ensemble, a heterogeneous mixture of compact and extended polypeptides, forms in a millisecond, substantially slower than the approximately 100-mus formation of a burst-phase intermediate in cytochrome c. The surprising finding is that, unlike for cytochrome c, there is an observable folding intermediate, but no microsecond burst phase in the folding kinetics of the structurally related thermostable protein.
Snapshots of a protein folding intermediate.,Yamada S, Bouley Ford ND, Keller GE, Ford WC, Gray HB, Winkler JR Proc Natl Acad Sci U S A. 2013 Jan 29;110(5):1606-10. doi:, 10.1073/pnas.1221832110. Epub 2013 Jan 14. PMID:23319660[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yamada S, Bouley Ford ND, Keller GE, Ford WC, Gray HB, Winkler JR. Snapshots of a protein folding intermediate. Proc Natl Acad Sci U S A. 2013 Jan 29;110(5):1606-10. doi:, 10.1073/pnas.1221832110. Epub 2013 Jan 14. PMID:23319660 doi:http://dx.doi.org/10.1073/pnas.1221832110
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