1cce: Difference between revisions

Latest revision as of 05:33, 13 August 2026

CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGENOUS LIGAND

Structural highlights

1cce is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:	HEM
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CCPR_YEAST Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

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

The crystal structure of the His-175-->Gly (H175G) mutant of cytochrome-c peroxidase (EC 1.11.1.5), missing its only heme ligand, reveals that the histidine is replaced by solvent to give a bisaquo heme protein. This protein retains some residual activity, which can be stimulated or inhibited by addition of exogenous ligands. Structural analysis confirms the binding of imidazole to the heme at the position of the wild-type histidine ligand. This imidazole complex reacts readily with hydrogen peroxide to produce a radical species with novel properties. However, reactivation in this complex is incomplete (approximately 5%), which, in view of the very similar structures of the wild-type and the H175G/imidazole forms, implies a critical role for tethering of the axial ligand in catalysis. This study demonstrates the feasibility of constructing heme enzymes with no covalent link to the protein and with unnatural ligand replacements. Such enzymes may prove useful in studies of electron transfer mechanisms and in the engineering of novel heme-based catalysts.

Construction of a bisaquo heme enzyme and binding by exogenous ligands.,McRee DE, Jensen GM, Fitzgerald MM, Siegel HA, Goodin DB Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12847-51. PMID:7809133^[1]

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

References

↑ McRee DE, Jensen GM, Fitzgerald MM, Siegel HA, Goodin DB. Construction of a bisaquo heme enzyme and binding by exogenous ligands. Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12847-51. PMID:7809133

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] McRee DE, Jensen GM, Fitzgerald MM, Siegel HA, Goodin DB. Construction of a bisaquo heme enzyme and binding by exogenous ligands. Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12847-51. PMID:7809133

[1]

@@ Line 1: / Line 1: @@
-[[Image:1cce.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1cce", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_1cce|  PDB=1cce  |  SCENE=  }}
-'''CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGENOUS LIGAND'''
+==CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGENOUS LIGAND==
+<StructureSection load='1cce' size='340' side='right'caption='[[1cce]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1cce]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CCE FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cce OCA], [https://pdbe.org/1cce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cce RCSB], [https://www.ebi.ac.uk/pdbsum/1cce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cce ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
+== 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/cc/1cce_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1cce ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The crystal structure of the His-175--&gt;Gly (H175G) mutant of cytochrome-c peroxidase (EC 1.11.1.5), missing its only heme ligand, reveals that the histidine is replaced by solvent to give a bisaquo heme protein. This protein retains some residual activity, which can be stimulated or inhibited by addition of exogenous ligands. Structural analysis confirms the binding of imidazole to the heme at the position of the wild-type histidine ligand. This imidazole complex reacts readily with hydrogen peroxide to produce a radical species with novel properties. However, reactivation in this complex is incomplete (approximately 5%), which, in view of the very similar structures of the wild-type and the H175G/imidazole forms, implies a critical role for tethering of the axial ligand in catalysis. This study demonstrates the feasibility of constructing heme enzymes with no covalent link to the protein and with unnatural ligand replacements. Such enzymes may prove useful in studies of electron transfer mechanisms and in the engineering of novel heme-based catalysts.
-==Overview==
+Construction of a bisaquo heme enzyme and binding by exogenous ligands.,McRee DE, Jensen GM, Fitzgerald MM, Siegel HA, Goodin DB Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12847-51. PMID:7809133<ref>PMID:7809133</ref>
-The crystal structure of the His-175--&gt;Gly (H175G) mutant of cytochrome-c peroxidase (EC 1.11.1.5), missing its only heme ligand, reveals that the histidine is replaced by solvent to give a bisaquo heme protein. This protein retains some residual activity, which can be stimulated or inhibited by addition of exogenous ligands. Structural analysis confirms the binding of imidazole to the heme at the position of the wild-type histidine ligand. This imidazole complex reacts readily with hydrogen peroxide to produce a radical species with novel properties. However, reactivation in this complex is incomplete (approximately 5%), which, in view of the very similar structures of the wild-type and the H175G/imidazole forms, implies a critical role for tethering of the axial ligand in catalysis. This study demonstrates the feasibility of constructing heme enzymes with no covalent link to the protein and with unnatural ligand replacements. Such enzymes may prove useful in studies of electron transfer mechanisms and in the engineering of novel heme-based catalysts.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-CCE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CCE OCA].
+</div>
+<div class="pdbe-citations 1cce" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Construction of a bisaquo heme enzyme and binding by exogenous ligands., McRee DE, Jensen GM, Fitzgerald MM, Siegel HA, Goodin DB, Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12847-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7809133 7809133]
+*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
-[[Category: Cytochrome-c peroxidase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Single protein]]
+[[Category: Fitzgerald MM]]
-[[Category: Fitzgerald, M M.]]
+[[Category: Goodin DB]]
-[[Category: Goodin, D B.]]
+[[Category: Jensen GM]]
-[[Category: Jensen, G M.]]
+[[Category: Mcree DE]]
-[[Category: Mcree, D E.]]
+[[Category: Siegel HA]]
-[[Category: Siegel, H A.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:34:42 2008''

1cce: Difference between revisions

Latest revision as of 05:33, 13 August 2026

CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGENOUS LIGAND

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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