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4put

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==Crystal structure of the Arabidopsis thaliana TOP2 oligopeptidase==
==Crystal structure of the Arabidopsis thaliana TOP2 oligopeptidase==
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<StructureSection load='4put' size='340' side='right' caption='[[4put]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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<StructureSection load='4put' size='340' side='right'caption='[[4put]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4put]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PUT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4put]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PUT FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 3&#8491;</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/Oligopeptidase_A Oligopeptidase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.70 3.4.24.70] </span></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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4put FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4put OCA], [http://pdbe.org/4put PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4put RCSB], [http://www.ebi.ac.uk/pdbsum/4put PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4put 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=4put FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4put OCA], [https://pdbe.org/4put PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4put RCSB], [https://www.ebi.ac.uk/pdbsum/4put PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4put ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/COPDA_ARATH COPDA_ARATH]] Oligopeptidase that may be involved in the degradation of proteasome-generated peptides (By similarity). Binds salicylic acid.<ref>PMID:24004003</ref> <ref>PMID:24043784</ref>
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[https://www.uniprot.org/uniprot/COPDA_ARATH COPDA_ARATH] Oligopeptidase that may be involved in the degradation of proteasome-generated peptides (By similarity). Binds salicylic acid.<ref>PMID:24004003</ref> <ref>PMID:24043784</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Thimet oligopeptidase (TOP) is a zinc-dependent metallopeptidase. Recent studies suggest that Arabidopsis thaliana TOP1 and TOP2 are targets for salicylic acid (SA) binding and participate in SA-mediated plant innate immunity. The crystal structure of A. thaliana TOP2 has been determined at 3.0 A resolution. Comparisons to the structure of human TOP revealed good overall structural conservation, especially in the active-site region, despite their weak sequence conservation. The protein sample was incubated with the photo-activated SA analog 4-azido-SA and exposed to UV irradiation before crystallization. However, there was no conclusive evidence for the binding of SA based on the X-ray diffraction data. Further studies are needed to elucidate the molecular mechanism of how SA regulates the activity of A. thaliana TOP1 and TOP2.
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Structure of the Arabidopsis thaliana TOP2 oligopeptidase.,Wang R, Rajagopalan K, Sadre-Bazzaz K, Moreau M, Klessig DF, Tong L Acta Crystallogr F Struct Biol Commun. 2014 May;70(Pt 5):555-9. doi:, 10.1107/S2053230X14006128. Epub 2014 Apr 15. PMID:24817709<ref>PMID:24817709</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 4put" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Oligopeptidase A]]
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[[Category: Arabidopsis thaliana]]
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[[Category: Rajagopalan, K]]
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[[Category: Large Structures]]
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[[Category: Tong, L]]
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[[Category: Rajagopalan K]]
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[[Category: Wang, R]]
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[[Category: Tong L]]
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[[Category: Hydrolase]]
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[[Category: Wang R]]
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[[Category: Oligopeptidase]]
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Current revision

Crystal structure of the Arabidopsis thaliana TOP2 oligopeptidase

PDB ID 4put

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