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| | <StructureSection load='4put' size='340' side='right'caption='[[4put]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='4put' size='340' side='right'caption='[[4put]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4put]] 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=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> | + | <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> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYOP, TOP2, At5g10540, F12B17.110 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <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> |
| - | <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>
| + | <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> |
| - | <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> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [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> |
| - | <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®/PubMed®, 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> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Oligopeptidase A]]
| + | [[Category: Rajagopalan K]] |
| - | [[Category: Rajagopalan, K]] | + | [[Category: Tong L]] |
| - | [[Category: Tong, L]] | + | [[Category: Wang R]] |
| - | [[Category: Wang, R]] | + | |
| - | [[Category: Hydrolase]]
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| - | [[Category: Oligopeptidase]]
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