5UK3
Crystal structure of cyanase from T. urticae
Summary for 5UK3
| Entry DOI | 10.2210/pdb5uk3/pdb |
| Descriptor | Uncharacterized protein (2 entities in total) |
| Functional Keywords | tetranychus urticae, cyanase, agricultural pest, two-spotted spidermite, spider mite, lyase |
| Biological source | Tetranychus urticae (Two-spotted spider mite) |
| Total number of polymer chains | 10 |
| Total formula weight | 202410.80 |
| Authors | Schlachter, C.R.,Chruszcz, M. (deposition date: 2017-01-19, release date: 2017-06-21, Last modification date: 2023-10-04) |
| Primary citation | Schlachter, C.R.,Klapper, V.,Wybouw, N.,Radford, T.,Van Leeuwen, T.,Grbic, M.,Chruszcz, M. Structural Characterization of a Eukaryotic Cyanase from Tetranychus urticae. J. Agric. Food Chem., 65:5453-5462, 2017 Cited by PubMed Abstract: 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. PubMed: 28613863DOI: 10.1021/acs.jafc.7b01333 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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