5uk3
From Proteopedia
(Difference between revisions)
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of cyanase from T. urticae== | |
| + | <StructureSection load='5uk3' size='340' side='right'caption='[[5uk3]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5uk3]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetranychus_urticae Tetranychus urticae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UK3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=5uk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uk3 OCA], [https://pdbe.org/5uk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uk3 RCSB], [https://www.ebi.ac.uk/pdbsum/5uk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uk3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/T1KZQ3_TETUR T1KZQ3_TETUR] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The two-spotted spider mite Tetranychus urticae is a polyphagous agricultural pest and poses a high risk to global crop production as it is rapidly developing pesticide resistance. Genomic and transcriptomic analysis has revealed the presence of a remarkable cyanase gene in T. urticae and related mite species within the Acariformes lineage. Cyanase catalyzes the detoxification of cyanate and is potentially an attractive protein target for the development of new acaricides. Phylogenetic analysis indicates that within the Acariformes, the cyanase gene originates from a single horizontal gene transfer event, which precedes subsequent speciation. Our structural studies presented here compare and contrast prokaryotic cyanases to T. urticae cyanase, which all form homodecamers and have conserved active site residues, but display different surface areas between homodimers in the overall decameric structure. | ||
| - | + | Structural Characterization of a Eukaryotic Cyanase from Tetranychus urticae.,Schlachter CR, Klapper V, Wybouw N, Radford T, Van Leeuwen T, Grbic M, Chruszcz M J Agric Food Chem. 2017 Jul 12;65(27):5453-5462. doi: 10.1021/acs.jafc.7b01333., Epub 2017 Jun 30. PMID:28613863<ref>PMID:28613863</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5uk3" style="background-color:#fffaf0;"></div> |
| - | [[Category: Chruszcz | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Tetranychus urticae]] | ||
| + | [[Category: Chruszcz M]] | ||
| + | [[Category: Schlachter CR]] | ||
Current revision
Crystal structure of cyanase from T. urticae
| |||||||||||
