View source for 5zg5


==Crystal Structure of Triosephosphate isomerase SADsubAAA mutant from Opisthorchis viverrini==
<StructureSection load='5zg5' size='340' side='right'caption='[[5zg5]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zg5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Opisthorchis_viverrini Opisthorchis viverrini]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZG5 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]] 1.597&#8491;</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=5zg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zg5 OCA], [https://pdbe.org/5zg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zg5 RCSB], [https://www.ebi.ac.uk/pdbsum/5zg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zg5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A074Z863_9TREM A0A074Z863_9TREM] 
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== Publication Abstract from PubMed ==
Opisthorchis viverrini, a parasitic trematode, was recategorized as a group 1 biological carcinogen because it causes opisthorchiasis, which may result in cholangiocarcinoma. A new strategy for controlling opisthorchiasis is needed because of issues such as drug resistance and reinfection. Triosephosphate isomerase (TIM), a key enzyme in energy metabolism, is regarded as a potential drug target and vaccine candidate against various pathogens. Here, we determined the crystal structures of wild-type and 3 variants of TIMs from O. viverrini (OvTIM) at high resolution. The unique tripeptide of parasite trematodes, the SAD motif, was located on the surface of OvTIM and contributed to forming a 310-helix of the following loop in a sequence-independent manner. Through thermal stability and structural analyses of OvTIM variants, we found that the SAD motif induced local structural alterations of the surface and was involved in the overall stability of OvTIM in a complementary manner with another parasite-specific residue, N115. Comparison of the surface characteristics between OvTIM and Homo sapiens TIM (HsTIM) and structure-based epitope prediction suggested that the SAD motif functions as an epitope.

Structural Analysis of an Epitope Candidate of Triosephosphate Isomerase in Opisthorchis viverrini.,Son J, Kim S, Kim SE, Lee H, Lee MR, Hwang KY Sci Rep. 2018 Oct 10;8(1):15075. doi: 10.1038/s41598-018-33479-8. PMID:30305716<ref>PMID:30305716</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zg5" style="background-color:#fffaf0;"></div>

==See Also==
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Opisthorchis viverrini]]
[[Category: Hwang KY]]
[[Category: Kim S]]
[[Category: Kim SE]]
[[Category: Lee H]]
[[Category: Lee MR]]
[[Category: Son J]]