4put
From Proteopedia
(Difference between revisions)
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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. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PUT OCA]. <br> | + | <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> |
</td></tr><tr><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><br> | </td></tr><tr><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><br> | ||
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ | + | <tr><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><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://www.rcsb.org/pdb/explore.do?structureId=4put RCSB], [http://www.ebi.ac.uk/pdbsum/4put PDBsum]</span></td></tr> | <tr><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://www.rcsb.org/pdb/explore.do?structureId=4put RCSB], [http://www.ebi.ac.uk/pdbsum/4put PDBsum]</span></td></tr> | ||
<table> | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 05:15, 25 June 2014
Crystal structure of the Arabidopsis thaliana TOP2 oligopeptidase
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