7ccp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="7ccp" size="450" color="white" frame="true" align="right" spinBox="true" caption="7ccp, resolution 2.2&Aring;" /> '''EFFECT OF ARGININE-48...)
Current revision (14:51, 6 March 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:7ccp.gif|left|200px]]<br /><applet load="7ccp" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="7ccp, resolution 2.2&Aring;" />
 
-
'''EFFECT OF ARGININE-48 REPLACEMENT ON THE REACTION BETWEEN CYTOCHROME C PEROXIDASE AND HYDROGEN PEROXIDE'''<br />
 
-
==Overview==
+
==EFFECT OF ARGININE-48 REPLACEMENT ON THE REACTION BETWEEN CYTOCHROME C PEROXIDASE AND HYDROGEN PEROXIDE==
-
The crystallographic structures of two cytochrome c peroxidase (CcP), mutants, CcP(R48L) and CcP(R48K), have been determined. In addition, the, electronic absorption spectrum and the hydrogen peroxide reactivity of, these two mutants have been determined between pH 4 and 8. Both the, crystallographic structure and the electronic absorption spectrum of, CcP(R48L) are consistent with exclusive pentacoordination of the heme iron, between pH 4 and 6.5. At higher pH, CcP(R48L) forms an alkaline, bis-imidazole form of CcP with the distal histidine coordinated to the, heme iron. The apparent pKA for this transition is 7.5 in CcP(R48L). The, observed pseudo-first-order rate constant for the reaction between, CcP(R48L) and hydrogen peroxide saturates at high peroxide concentrations., The data are consistent with a rate-limiting oxygen-oxygen bond scission, at high peroxide concentrations. The observed rate of the bond scission, step ranges between 1000 and 1950 s-1, an estimated 2 orders of magnitude, slower than for wild-type enzyme. The data suggest that the protonated, form of His-52 increases the bond scission step by a factor of 2. The, properties of the CcP(R48K) mutant are significantly different from those, of CcP(R48L). The crystal structure of CcP(R48K) shows Lys-48 occupying, the putative peroxide binding site. The electronic absorption spectrum, indicates that CcP(R48K) is predominantly pentacoordinate at neutral pH, but with detectable amounts of hexacoordinate forms. Two ionizable groups, affect the electronic absorption spectrum of CcP(R48K). An apparent, ionization near pH 4 produces an enzyme with increased hexacoordination, while an apparent pKA of 6.9 generates the alkaline bis-imidazole form., The peroxide reaction saturates at high peroxide concentrations for, CcP(R48K) and is attributed to a conformational-gating mechanism. The, maximum rate for the reaction between CcP(R48K) and hydrogen peroxide is, probably limited by the movement of either Lys-48 or His-52. This rate is, 200 and 290 s-1 in nitrate-containing buffers and phosphate buffers, respectively. Evidence is provided that Arg-48 in wild-type enzyme is, responsible for nitrate binding in the heme pocket and for stabilizing CcP, Compound I.
+
<StructureSection load='7ccp' size='340' side='right'caption='[[7ccp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[7ccp]] 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=7CCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CCP 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]] 2.2&#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=7ccp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ccp OCA], [https://pdbe.org/7ccp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ccp RCSB], [https://www.ebi.ac.uk/pdbsum/7ccp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ccp 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/7ccp_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=7ccp ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
7CCP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=7CCP OCA].
+
*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Effect of arginine-48 replacement on the reaction between cytochrome c peroxidase and hydrogen peroxide., Vitello LB, Erman JE, Miller MA, Wang J, Kraut J, Biochemistry. 1993 Sep 21;32(37):9807-18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8396973 8396973]
+
[[Category: Large Structures]]
-
[[Category: Cytochrome-c peroxidase]]
+
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
-
[[Category: Single protein]]
+
[[Category: Kraut J]]
-
[[Category: Kraut, J.]]
+
[[Category: Miller MA]]
-
[[Category: Miller, M.A.]]
+
[[Category: Wang J]]
-
[[Category: Wang, J.]]
+
-
[[Category: HEM]]
+
-
[[Category: oxidoreductase(h2o2(a))]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:20:06 2007''
+

Current revision

EFFECT OF ARGININE-48 REPLACEMENT ON THE REACTION BETWEEN CYTOCHROME C PEROXIDASE AND HYDROGEN PEROXIDE

PDB ID 7ccp

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7ccp"
Personal tools