1qyz

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[[Image:1qyz.jpg|left|200px]]
 
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{{Structure
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==Characterization of the malformed, recombinant cytochrome rC552==
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|PDB= 1qyz |SIZE=350|CAPTION= <scene name='initialview01'>1qyz</scene>, resolution 1.40&Aring;
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<StructureSection load='1qyz' size='340' side='right'caption='[[1qyz]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=HCO:2-ACETYL-PROTOPORPHYRIN+IX'>HCO</scene>
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<table><tr><td colspan='2'>[[1qyz]] 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=1QYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QYZ FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.4&#8491;</td></tr>
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|GENE= CYCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HCO:2-ACETYL-PROTOPORPHYRIN+IX'>HCO</scene></td></tr>
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|DOMAIN=
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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=1qyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qyz OCA], [https://pdbe.org/1qyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qyz RCSB], [https://www.ebi.ac.uk/pdbsum/1qyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qyz ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qyz OCA], [http://www.ebi.ac.uk/pdbsum/1qyz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qyz RCSB]</span>
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== Function ==
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}}
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[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.
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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/qy/1qyz_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=1qyz 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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Expression of the truncated (lacking an N-terminal signal sequence) structural gene of Thermus thermophilus cytochrome c(552) in the cytoplasm of Escherichia coli yields both dimeric (rC(557)) and monomeric (rC(552)) cytochrome c-like proteins [Keightley, J. A., et al. (1998) J. Biol. Chem. 273, 12006-12016], which form spontaneously without the involvement of cytochrome c maturation factors. Cytochrome rC(557) is comprised of a dimer and has been structurally characterized [McRee, D., et al. (2001) J. Biol. Chem. 276, 6537-6544]. Unexpectedly, the monomeric rC(552) transforms spontaneously to a cytochrome-like chromophore having, in its reduced state, the Q(oo) transition (alpha-band) at 572 nm (therefore called p572). The X-ray crystallographic structure of rC(552), at 1.41 A resolution, shows that the 2-vinyl group of heme ring I is converted to a [heme-CO-CH(2)-S-CH(2)-C(alpha)] conjugate with cysteine 11. Electron density maps obtained from isomorphous crystals of p572 at 1.61 A resolution reveal that the 2-vinyl group has been oxidized to a formyl group. This explains the lower energy of the Q(oo)() transition, the presence of a new, high-frequency band in the resonance Raman spectra at 1666 cm(-1) for oxidized and at 1646 cm(-1) for reduced samples, and the greatly altered, paramagnetically shifted (1)H NMR spectrum observed for this species. The overall process defines a novel mechanism for oxidation of the 2-vinyl group to a 2-formyl group and adds to the surprising array of chemical reactions that occur in the interaction of heme with the CXXCH sequence motif in apocytochromes c.
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'''Characterization of the malformed, recombinant cytochrome rC552'''
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Cytochrome rC552, formed during expression of the truncated, Thermus thermophilus cytochrome c552 gene in the cytoplasm of Escherichia coli, reacts spontaneously to form protein-bound 2-formyl-4-vinyl (Spirographis) heme.,Fee JA, Todaro TR, Luna E, Sanders D, Hunsicker-Wang LM, Patel KM, Bren KL, Gomez-Moran E, Hill MG, Ai J, Loehr TM, Oertling WA, Williams PA, Stout CD, McRee D, Pastuszyn A Biochemistry. 2004 Sep 28;43(38):12162-76. PMID:15379555<ref>PMID:15379555</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1qyz" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Expression of the truncated (lacking an N-terminal signal sequence) structural gene of Thermus thermophilus cytochrome c(552) in the cytoplasm of Escherichia coli yields both dimeric (rC(557)) and monomeric (rC(552)) cytochrome c-like proteins [Keightley, J. A., et al. (1998) J. Biol. Chem. 273, 12006-12016], which form spontaneously without the involvement of cytochrome c maturation factors. Cytochrome rC(557) is comprised of a dimer and has been structurally characterized [McRee, D., et al. (2001) J. Biol. Chem. 276, 6537-6544]. Unexpectedly, the monomeric rC(552) transforms spontaneously to a cytochrome-like chromophore having, in its reduced state, the Q(oo) transition (alpha-band) at 572 nm (therefore called p572). The X-ray crystallographic structure of rC(552), at 1.41 A resolution, shows that the 2-vinyl group of heme ring I is converted to a [heme-CO-CH(2)-S-CH(2)-C(alpha)] conjugate with cysteine 11. Electron density maps obtained from isomorphous crystals of p572 at 1.61 A resolution reveal that the 2-vinyl group has been oxidized to a formyl group. This explains the lower energy of the Q(oo)() transition, the presence of a new, high-frequency band in the resonance Raman spectra at 1666 cm(-1) for oxidized and at 1646 cm(-1) for reduced samples, and the greatly altered, paramagnetically shifted (1)H NMR spectrum observed for this species. The overall process defines a novel mechanism for oxidation of the 2-vinyl group to a 2-formyl group and adds to the surprising array of chemical reactions that occur in the interaction of heme with the CXXCH sequence motif in apocytochromes c.
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*[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]]
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== References ==
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==About this Structure==
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<references/>
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1QYZ 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=1QYZ OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Cytochrome rC552, formed during expression of the truncated, Thermus thermophilus cytochrome c552 gene in the cytoplasm of Escherichia coli, reacts spontaneously to form protein-bound 2-formyl-4-vinyl (Spirographis) heme., Fee JA, Todaro TR, Luna E, Sanders D, Hunsicker-Wang LM, Patel KM, Bren KL, Gomez-Moran E, Hill MG, Ai J, Loehr TM, Oertling WA, Williams PA, Stout CD, McRee D, Pastuszyn A, Biochemistry. 2004 Sep 28;43(38):12162-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15379555 15379555]
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[[Category: Single protein]]
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[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Ai, J.]]
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[[Category: Ai J]]
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[[Category: Bren, K L.]]
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[[Category: Bren KL]]
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[[Category: Fee, J A.]]
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[[Category: Fee JA]]
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[[Category: Gomez-Moran, E.]]
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[[Category: Gomez-Moran E]]
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[[Category: Hill, M G.]]
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[[Category: Hill MG]]
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[[Category: Hunsicker-Wang, L M.]]
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[[Category: Hunsicker-Wang LM]]
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[[Category: Loehr, T M.]]
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[[Category: Loehr TM]]
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[[Category: Luna, E.]]
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[[Category: Luna E]]
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[[Category: McRee, D.]]
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[[Category: McRee D]]
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[[Category: Oertling, W A.]]
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[[Category: Oertling WA]]
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[[Category: Pastuszyn, A.]]
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[[Category: Pastuszyn A]]
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[[Category: Patel, K M.]]
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[[Category: Patel KM]]
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[[Category: Sanders, D.]]
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[[Category: Sanders D]]
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[[Category: Stout, C D.]]
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[[Category: Stout CD]]
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[[Category: Todaro, T R.]]
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[[Category: Todaro TR]]
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[[Category: Williams, P A.]]
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[[Category: Williams PA]]
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[[Category: malformed cytochrome c]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:20:59 2008''
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Current revision

Characterization of the malformed, recombinant cytochrome rC552

PDB ID 1qyz

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