7chi

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<StructureSection load='7chi' size='340' side='right'caption='[[7chi]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='7chi' size='340' side='right'caption='[[7chi]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7chi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CHI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7CHI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7chi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CHI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PCO5, At3g58670, T20N10.20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PCO5, At3g58670, T20N10.20 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine_dioxygenase Cysteine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.20 1.13.11.20] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cysteine_dioxygenase Cysteine dioxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.20 1.13.11.20] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7chi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7chi OCA], [http://pdbe.org/7chi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7chi RCSB], [http://www.ebi.ac.uk/pdbsum/7chi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7chi ProSAT]</span></td></tr>
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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=7chi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7chi OCA], [https://pdbe.org/7chi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7chi RCSB], [https://www.ebi.ac.uk/pdbsum/7chi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7chi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PCO5_ARATH PCO5_ARATH]] Oxidizes N-terminal cysteine residues, thus preparing the protein for N-end rule pathway-mediated proteasomal degradation.<ref>PMID:24599061</ref>
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[[https://www.uniprot.org/uniprot/PCO5_ARATH PCO5_ARATH]] Oxidizes N-terminal cysteine residues, thus preparing the protein for N-end rule pathway-mediated proteasomal degradation.<ref>PMID:24599061</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Plant Cysteine Oxidases (PCOs) play important roles in controlling the stability of Group VII ethylene response factors (ERF-VIIs) via Arg/N-degron pathway through catalyzing the oxidation of their N-Cys for subsequent Arginyl-tRNA--protein transferase 1 (ATE1) mediated arginine installation. Here we presented the crystal structures of PCO2, PCO4, and PCO5 from Arabidopsis thaliana (AtPCOs) and examined their in vitro activity by Mass spectrometry (MS). On the basis of Tris-bound AtPCO2, we modelled the structure of Cys-bound AtPCO2 and identified key AtPCO2 residues involved in N-Cys recognition and oxidation. Alanine substitution of potential N-Cys interaction residues impaired the activity of AtPCO5 remarkably. The structural research, complemented by mutagenesis and MS experiments, not only uncovers the substrate recognition and catalytic mode by AtPCOs, but also sheds light on the future design of potent inhibitors for plant cysteine oxidases.
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Molecular basis for cysteine oxidation by plant cysteine oxidases from Arabidopsis thaliana.,Chen Z, Guo Q, Wu G, Wen J, Liao S, Xu C J Struct Biol. 2021 Mar;213(1):107663. doi: 10.1016/j.jsb.2020.107663. Epub 2020 , Nov 15. PMID:33207269<ref>PMID:33207269</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 7chi" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 10:47, 31 March 2021

crystal structure of pco5

PDB ID 7chi

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