5vg2: Difference between revisions
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The | ==Intradiol ring-cleavage Dioxygenase from Tetranychus urticae== | ||
<StructureSection load='5vg2' size='340' side='right'caption='[[5vg2]], [[Resolution|resolution]] 2.46Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5vg2]] is a 4 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=5VG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VG2 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]] 2.46Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=5vg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vg2 OCA], [https://pdbe.org/5vg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vg2 RCSB], [https://www.ebi.ac.uk/pdbsum/5vg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vg2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/T1K8P1_TETUR T1K8P1_TETUR] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Genome analyses of the polyphagous spider mite herbivore Tetranychus urticae (two-spotted spider mite) revealed the presence of a set of 17 genes that code for secreted proteins belonging to the "intradiol dioxygenase-like" subgroup. Phylogenetic analyses indicate that this novel enzyme family has been acquired by horizontal gene transfer. In order to better understand the role of these proteins in T. urticae, we have structurally and functionally characterized one paralog (tetur07g02040). It was demonstrated that this protein is indeed an intradiol ring-cleavage dioxygenase, as the enzyme is able to cleave catechol between two hydroxyl-groups using atmospheric dioxygen. The enzyme was characterized functionally and structurally. The active site of the T. urticae enzyme contains an Fe(3+) cofactor that is coordinated by two histidine and two tyrosine residues, an arrangement that is similar to those observed in bacterial homologs. However, the active site is significantly more solvent exposed than in bacterial proteins. Moreover, the mite enzyme is monomeric, while almost all structurally characterized bacterial homologs form oligomeric assemblies. Tetur07g02040 is not only the first spider mite dioxygenase that has been characterized at the molecular level, but is also the first structurally characterized intradiol ring-cleavage dioxygenase originating from a eukaryote. | |||
Structural and functional characterization of an intradiol ring-cleavage dioxygenase from the polyphagous spider mite herbivore Tetranychus urticae Koch.,Schlachter CR, Daneshian L, Amaya J, Klapper V, Wybouw N, Borowski T, Van Leeuwen T, Grbic V, Grbic M, Makris TM, Chruszcz M Insect Biochem Mol Biol. 2019 Apr;107:19-30. doi: 10.1016/j.ibmb.2018.12.001., Epub 2018 Dec 5. PMID:30529144<ref>PMID:30529144</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5vg2" style="background-color:#fffaf0;"></div> | ||
[[Category: Chruszcz | |||
[[Category: Schlachter | ==See Also== | ||
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Tetranychus urticae]] | |||
[[Category: Chruszcz M]] | |||
[[Category: Klapper V]] | |||
[[Category: Schlachter C]] | |||
Latest revision as of 16:48, 4 October 2023
Intradiol ring-cleavage Dioxygenase from Tetranychus urticaeIntradiol ring-cleavage Dioxygenase from Tetranychus urticae
Structural highlights
FunctionPublication Abstract from PubMedGenome analyses of the polyphagous spider mite herbivore Tetranychus urticae (two-spotted spider mite) revealed the presence of a set of 17 genes that code for secreted proteins belonging to the "intradiol dioxygenase-like" subgroup. Phylogenetic analyses indicate that this novel enzyme family has been acquired by horizontal gene transfer. In order to better understand the role of these proteins in T. urticae, we have structurally and functionally characterized one paralog (tetur07g02040). It was demonstrated that this protein is indeed an intradiol ring-cleavage dioxygenase, as the enzyme is able to cleave catechol between two hydroxyl-groups using atmospheric dioxygen. The enzyme was characterized functionally and structurally. The active site of the T. urticae enzyme contains an Fe(3+) cofactor that is coordinated by two histidine and two tyrosine residues, an arrangement that is similar to those observed in bacterial homologs. However, the active site is significantly more solvent exposed than in bacterial proteins. Moreover, the mite enzyme is monomeric, while almost all structurally characterized bacterial homologs form oligomeric assemblies. Tetur07g02040 is not only the first spider mite dioxygenase that has been characterized at the molecular level, but is also the first structurally characterized intradiol ring-cleavage dioxygenase originating from a eukaryote. Structural and functional characterization of an intradiol ring-cleavage dioxygenase from the polyphagous spider mite herbivore Tetranychus urticae Koch.,Schlachter CR, Daneshian L, Amaya J, Klapper V, Wybouw N, Borowski T, Van Leeuwen T, Grbic V, Grbic M, Makris TM, Chruszcz M Insect Biochem Mol Biol. 2019 Apr;107:19-30. doi: 10.1016/j.ibmb.2018.12.001., Epub 2018 Dec 5. PMID:30529144[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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