3e2n

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{{Seed}}
 
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[[Image:3e2n.png|left|200px]]
 
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==Engineering ascorbate peroxidase activity into cytochrome c peroxidase==
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The line below this paragraph, containing "STRUCTURE_3e2n", creates the "Structure Box" on the page.
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<StructureSection load='3e2n' size='340' side='right'caption='[[3e2n]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3e2n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E2N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E2N FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#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></td></tr>
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{{STRUCTURE_3e2n| PDB=3e2n | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e2n OCA], [https://pdbe.org/3e2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e2n RCSB], [https://www.ebi.ac.uk/pdbsum/3e2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e2n ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/APX1_PEA APX1_PEA] Plays a key role in hydrogen peroxide removal.[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e2/3e2n_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3e2n ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cytochrome c peroxidase (CCP) and ascorbate peroxidase (APX) have very similar structures, and yet neither CCP nor APX exhibits each other's activities with respect to reducing substrates. APX has a unique substrate binding site near the heme propionates where ascorbate H-bonds with a surface Arg and one heme propionate (Sharp et al. (2003) Nat. Struct. Biol. 10, 303-307). The corresponding region in CCP has a much longer surface loop, and the critical Arg residue that is required for ascorbate binding in APX is Asn in CCP. In order to convert CCP into an APX, the ascorbate-binding loop and critical arginine were engineered into CCP to give the CCP2APX mutant. The mutant crystal structure shows that the engineered site is nearly identical to that found in APX. While wild-type CCP shows no APX activity, CCP2APX catalyzes the peroxidation of ascorbate at a rate of approximately 12 min (-1), indicating that the engineered ascorbate-binding loop can bind ascorbate.
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===Engineering ascorbate peroxidase activity into cytochrome c peroxidase===
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Engineering ascorbate peroxidase activity into cytochrome c peroxidase.,Meharenna YT, Oertel P, Bhaskar B, Poulos TL Biochemistry. 2008 Sep 30;47(39):10324-32. Epub 2008 Sep 5. PMID:18771292<ref>PMID:18771292</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3e2n" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18771292}}, adds the Publication Abstract to the page
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*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18771292 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18771292}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3E2N 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=3E2N OCA].
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[[Category: Pisum sativum]]
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==Reference==
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<ref group="xtra">PMID:18771292</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Meharenna, Y T.]]
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[[Category: Meharenna YT]]
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[[Category: Oertel, P.]]
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[[Category: Oertel P]]
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[[Category: Poulos, T L.]]
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[[Category: Poulos TL]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:45:40 2009''
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Current revision

Engineering ascorbate peroxidase activity into cytochrome c peroxidase

PDB ID 3e2n

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