1stq: Difference between revisions

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{{Seed}}
[[Image:1stq.png|left|200px]]


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==Cyrstal Structure of Cytochrome c Peroxidase Mutant: CcPK2M3==
The line below this paragraph, containing "STRUCTURE_1stq", creates the "Structure Box" on the page.
<StructureSection load='1stq' size='340' side='right'caption='[[1stq]], [[Resolution|resolution]] 1.82&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'>[[1stq]] 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=1STQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1STQ 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]] 1.82&#8491;</td></tr>
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<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>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
{{STRUCTURE_1stq|  PDB=1stq  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1stq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1stq OCA], [https://pdbe.org/1stq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1stq RCSB], [https://www.ebi.ac.uk/pdbsum/1stq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1stq 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/st/1stq_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=1stq ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Previously a K(+)-binding site, analogous to that found in ascorbate peroxidase (APX), was engineered into cytochrome c peroxidase (CcP) to test the hypothesis that the bound K(+) influences the stability of the Trp191 cation radical formed during the CcP catalytic cycle (Bonagura et al., (1996) Biochemistry 35, 6107 and Bonagura et al., (1999) Biochemistry 38, 5528). Characterization of this mutant, designated CcPK2, showed that the stability of the Trp191 cation radical is dependent on the occupancy of the engineered K(+) site and that the Trp191 radical was much less stable in this mutant than in wild-type CcP. The mutations Met230Leu, Met231Gln, and Met172Ser have now been constructed on the CcPK2 mutant template to test if the Met residues also contribute to the stabilization of the Trp191 cation radical. Crystal structures show that the mutations affect only the local structure near the sites of mutation. Removal of these electronegative residues located less than 8 A from the Trp radical results in a further destabilization of the Trp radical. The characteristic EPR signal associated with the Trp radical is significantly narrowed and is characteristic of a tyrosine radical signal. Double-mixing stopped-flow experiments, where the delay time between the formation of CcP compound I and its mixing with horse heart ferrocytochrome c is varied, show that the stability of the Trp radical decreases as the Met residues are removed from the proximal cavity. When taken together, these results demonstrate a strong correlation between the experimentally determined stability of the Trp191 radical, the enzyme activity, and the calculated electrostatic stabilization of the Trp191 radical.


===Cyrstal Structure of Cytochrome c Peroxidase Mutant: CcPK2M3===
Electrostatic control of the tryptophan radical in cytochrome c peroxidase.,Barrows TP, Bhaskar B, Poulos TL Biochemistry. 2004 Jul 13;43(27):8826-34. PMID:15236591<ref>PMID:15236591</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1stq" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_15236591}}, adds the Publication Abstract to the page
*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 15236591 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_15236591}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1STQ is a 1 chain 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=1STQ OCA].
 
==Reference==
<ref group="xtra">PMID:15236591</ref><references group="xtra"/>
[[Category: Cytochrome-c peroxidase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Barrows, T P.]]
[[Category: Barrows TP]]
[[Category: Bhaskar, B.]]
[[Category: Bhaskar B]]
[[Category: Poulos, T L.]]
[[Category: Poulos TL]]
[[Category: Ccp]]
[[Category: Cytochrome c peroxidase]]
[[Category: Haem peroxidase]]
[[Category: Heme peroxidase]]
 
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Retrieved from "https://proteopedia.org/1stq"