1r0q

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[[Image:1r0q.png|left|200px]]
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==Characterization of the conversion of the malformed, recombinant cytochrome rc552 to a 2-formyl-4-vinyl (Spirographis) heme==
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<StructureSection load='1r0q' size='340' side='right' caption='[[1r0q]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1r0q]] is a 1 chain structure with 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=1R0Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R0Q FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HFM:2-FORMYL-PROTOPORPHRYN+IX'>HFM</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qyz|1qyz]]</td></tr>
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<tr><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 Thermus thermophilus])</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r0q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1r0q RCSB], [http://www.ebi.ac.uk/pdbsum/1r0q PDBsum]</span></td></tr>
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<table>
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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/r0/1r0q_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata 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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{{STRUCTURE_1r0q| PDB=1r0q | SCENE= }}
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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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===Characterization of the conversion of the malformed, recombinant cytochrome rc552 to a 2-formyl-4-vinyl (Spirographis) heme===
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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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{{ABSTRACT_PUBMED_15379555}}
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==About this Structure==
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[[1r0q]] is a 1 chain structure with 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=1R0Q OCA].
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==See Also==
==See Also==
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*[[Cytochrome c|Cytochrome c]]
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*[[Nitric reductase|Nitric reductase]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:015379555</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Ai, J.]]
[[Category: Ai, J.]]

Revision as of 20:06, 28 September 2014

Characterization of the conversion of the malformed, recombinant cytochrome rc552 to a 2-formyl-4-vinyl (Spirographis) heme

1r0q, resolution 1.61Å

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