1r0q

<StructureSection load='1r0q' size='340' side='right' caption='[[1r0q]], [[Resolution|resolution]] 1.61&Aring;' scene=''>

<table><tr><td colspan='2'>[[1r0q]] 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=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>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HFM:2-FORMYL-PROTOPORPHRYN+IX'>HFM</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qyz|1qyz]]</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='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=1r0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r0q OCA], [http://pdbe.org/1r0q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r0q RCSB], [http://www.ebi.ac.uk/pdbsum/1r0q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r0q ProSAT]</span></td></tr>

[[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.

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== Publication Abstract from PubMed ==

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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== References ==

[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]

[[Category: Ai, J]]

[[Category: Bren, K L]]

[[Category: Fee, J A]]

[[Category: Gomez-Moran, E]]

[[Category: Hill, M G]]

[[Category: Hunsicker-Wang, L M]]

[[Category: Loehr, T M]]

[[Category: Luna, E]]

[[Category: McRee, D]]

[[Category: Oertling, W A]]

[[Category: Pastuszyn, A]]

[[Category: Patel, K M]]

[[Category: Sanders, D]]

[[Category: Stout, C D]]

[[Category: Todaro, T R]]

[[Category: Williams, P A]]

[[Category: Oxidoreductase]]