1foc

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[[Image:1foc.gif|left|200px]]
 
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==Cytochrome C557: improperly folded thermus thermophilus C552==
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The line below this paragraph, containing "STRUCTURE_1foc", creates the "Structure Box" on the page.
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<StructureSection load='1foc' size='340' side='right'caption='[[1foc]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<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>
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{{STRUCTURE_1foc| PDB=1foc | SCENE= }}
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<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>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/1foc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1foc ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Cytochrome C557: improperly folded thermus thermophilus C552'''
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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<ref>PMID:11069913</ref>
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==Overview==
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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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1FOC is a [[Single protein]] structure of sequence 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=1FOC OCA].
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</div>
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<div class="pdbe-citations 1foc" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11069913 11069913]
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*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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[[Category: Single protein]]
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== References ==
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[[Category: Thermus thermophilus]]
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<references/>
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[[Category: Bren, K L.]]
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__TOC__
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[[Category: Fee, J A.]]
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</StructureSection>
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[[Category: McRee, D E.]]
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[[Category: Large Structures]]
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[[Category: Williams, P A.]]
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[[Category: Thermus thermophilus HB8]]
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[[Category: Cytochrome c]]
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[[Category: Bren KL]]
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[[Category: Heme inversion]]
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[[Category: Fee JA]]
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[[Category: Thermus thermophilus]]
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[[Category: McRee DE]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:34:13 2008''
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[[Category: Williams PA]]

Current revision

Cytochrome C557: improperly folded thermus thermophilus C552

PDB ID 1foc

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