This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1r0q

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:08, 17 April 2024) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1r0q.gif|left|200px]]
 
-
<!--
+
==Characterization of the conversion of the malformed, recombinant cytochrome rc552 to a 2-formyl-4-vinyl (Spirographis) heme==
-
The line below this paragraph, containing "STRUCTURE_1r0q", creates the "Structure Box" on the page.
+
<StructureSection load='1r0q' size='340' side='right'caption='[[1r0q]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1r0q]] 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=1R0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R0Q FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.61&#8491;</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>
-
{{STRUCTURE_1r0q| PDB=1r0q | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r0q OCA], [https://pdbe.org/1r0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r0q RCSB], [https://www.ebi.ac.uk/pdbsum/1r0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r0q ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[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.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r0/1r0q_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=1r0q ConSurf].
 +
<div style="clear:both"></div>
-
'''Characterization of the conversion of the malformed, recombinant cytochrome rc552 to a 2-formyl-4-vinyl (Spirographis) heme'''
+
==See Also==
-
 
+
*[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
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.
+
[[Category: Large Structures]]
-
 
+
-
==About this Structure==
+
-
1R0Q 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=1R0Q OCA].
+
-
 
+
-
==Reference==
+
-
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]
+
-
[[Category: Single protein]]
+
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
-
[[Category: Ai, J.]]
+
[[Category: Ai J]]
-
[[Category: Bren, K L.]]
+
[[Category: Bren KL]]
-
[[Category: Fee, J A.]]
+
[[Category: Fee JA]]
-
[[Category: Gomez-Moran, E.]]
+
[[Category: Gomez-Moran E]]
-
[[Category: Hill, M G.]]
+
[[Category: Hill MG]]
-
[[Category: Hunsicker-Wang, L M.]]
+
[[Category: Hunsicker-Wang LM]]
-
[[Category: Loehr, T M.]]
+
[[Category: Loehr TM]]
-
[[Category: Luna, E.]]
+
[[Category: Luna E]]
-
[[Category: McRee, D.]]
+
[[Category: McRee D]]
-
[[Category: Oertling, W A.]]
+
[[Category: Oertling WA]]
-
[[Category: Pastuszyn, A.]]
+
[[Category: Pastuszyn A]]
-
[[Category: Patel, K M.]]
+
[[Category: Patel KM]]
-
[[Category: Sanders, D.]]
+
[[Category: Sanders D]]
-
[[Category: Stout, C D.]]
+
[[Category: Stout CD]]
-
[[Category: Todaro, T R.]]
+
[[Category: Todaro TR]]
-
[[Category: Williams, P A.]]
+
[[Category: Williams PA]]
-
[[Category: Malformed cytochrome c]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:56:01 2008''
+

Current revision

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

PDB ID 1r0q

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools