3e2n: Difference between revisions
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<StructureSection load='3e2n' size='340' side='right'caption='[[3e2n]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='3e2n' size='340' side='right'caption='[[3e2n]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3e2n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> | ||
<tr id=' | <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=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> | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[https://www.uniprot.org/uniprot/CCPR_YEAST CCPR_YEAST | [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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pisum sativum]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: | [[Category: Meharenna YT]] | ||
[[Category: | [[Category: Oertel P]] | ||
[[Category: Poulos TL]] | |||
Latest revision as of 15:57, 30 August 2023
Engineering ascorbate peroxidase activity into cytochrome c peroxidaseEngineering ascorbate peroxidase activity into cytochrome c peroxidase
Structural highlights
FunctionAPX1_PEA Plays a key role in hydrogen peroxide removal.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 PubMedCytochrome 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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