1r0q

From Proteopedia

(Difference between revisions)

Revision as of 13:15, 16 December 2020

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

Structural highlights

1r0q is a 1 chain structure with sequence from "flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1qyz
Gene:	CYCA ("Flavobacterium thermophilum" Yoshida and Oshima 1971)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CY552_THETH] 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

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. 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. Biochemistry. 2004 Sep 28;43(38):12162-76. PMID:15379555 doi:10.1021/bi048968l

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1r0q"

@@ Line 1: / Line 1: @@
 ==Characterization of the conversion of the malformed, recombinant cytochrome rc552 to a 2-formyl-4-vinyl (Spirographis) heme==
-<StructureSection load='1r0q' size='340' side='right' caption='[[1r0q]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
+<StructureSection load='1r0q' size='340' side='right'caption='[[1r0q]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<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://proteopedia.org/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>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qyz|1qyz]]</div></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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
 </table>
 == Function ==
@@ Line 30: / Line 30: @@
 </div>
 <div class="pdbe-citations 1r0q" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Nitrite reductase 3D structures|Nitrite reductase 3D structures]]
 == References ==
 <references/>
@@ Line 35: / Line 38: @@
 </StructureSection>
 [[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
+[[Category: Large Structures]]
 [[Category: Ai, J]]
 [[Category: Bren, K L]]

1r0q

From Proteopedia

Revision as of 13:15, 16 December 2020

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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