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| | <StructureSection load='1foc' size='340' side='right'caption='[[1foc]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='1foc' size='340' side='right'caption='[[1foc]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1foc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FOC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1foc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FOC 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]] 3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dt1|1dt1]], [[1c52|1c52]]</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='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=1foc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1foc OCA], [http://pdbe.org/1foc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1foc RCSB], [http://www.ebi.ac.uk/pdbsum/1foc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1foc 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=1foc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1foc OCA], [https://pdbe.org/1foc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1foc RCSB], [https://www.ebi.ac.uk/pdbsum/1foc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1foc 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_THET8 CY552_THET8] This monoheme basic protein appears to function as an electron donor to cytochrome oxidase in T.thermophilus. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/1foc_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/1foc_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thet8]] | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Bren, K L]] | + | [[Category: Bren KL]] |
| - | [[Category: Fee, J A]] | + | [[Category: Fee JA]] |
| - | [[Category: McRee, D E]] | + | [[Category: McRee DE]] |
| - | [[Category: Williams, P A]] | + | [[Category: Williams PA]] |
| - | [[Category: Cytochrome c]]
| + | |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Heme inversion]]
| + | |
| - | [[Category: Thermus thermophilus]]
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| Structural highlights
Function
CY552_THET8 This monoheme basic protein appears to function as an electron donor to cytochrome oxidase in T.thermophilus.
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
Cytochrome rC(557) is an improperly matured, dimeric cytochrome c obtained from expression of the "signal peptide-lacking" Thermus thermophilus cycA gene in the cytoplasm of Escherichia coli. It is characterized by its Q(00) (or alpha-) optical absorption band at 557 nm in the reduced form (Keightley, J. A., Sanders, D., Todaro, T. R., Pastuszyn, A., and Fee, J. A. (1998) J. Biol. Chem. 273, 12006-12016). We report results of a broad ranging, biochemical and spectral characterization of this protein that reveals the presence of a free vinyl group on the porphyrin and a disulfide bond between the protomers and supports His-Met ligation in both valence states of the iron. A 3-A resolution x-ray structure shows that, in comparison with the native protein, the heme moiety is rotated 180 degrees about its alpha,gamma-axis; cysteine 14 has formed a thioether bond with the 2-vinyl of pyrrole ring I instead of the 4-vinyl of pyrrole ring II, as occurs in the native protein; and a cysteine 11 from each protomer has formed an intermolecular disulfide bond. Numerous, minor perturbations exist within the structure of rC(557) in comparison with that of native protein, which result from heme inversion and protein-protein interactions across the dimer interface. The unusual spectral properties of rC(557) are rationalized in terms of this structure.
Recombinant cytochrome rC557 obtained from Escherichia coli cells expressing a truncated Thermus thermophilus cycA gene. Heme inversion in an improperly matured protein.,McRee DE, Williams PA, Sridhar V, Pastuszyn A, Bren KL, Patel KM, Chen Y, Todaro TR, Sanders D, Luna E, Fee JA J Biol Chem. 2001 Mar 2;276(9):6537-44. Epub 2000 Nov 7. PMID:11069913[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ McRee DE, Williams PA, Sridhar V, Pastuszyn A, Bren KL, Patel KM, Chen Y, Todaro TR, Sanders D, Luna E, Fee JA. Recombinant cytochrome rC557 obtained from Escherichia coli cells expressing a truncated Thermus thermophilus cycA gene. Heme inversion in an improperly matured protein. J Biol Chem. 2001 Mar 2;276(9):6537-44. Epub 2000 Nov 7. PMID:11069913 doi:10.1074/jbc.M008421200
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