5ZG4

Crystal Structure of Triosephosphate isomerase SAD deletion mutant from Opisthorchis viverrini

5ZG4 の概要

• エントリーDOI: 10.2210/pdb5zg4/pdb
• 関連するPDBエントリー: 5ZFX
• 分子名称: Triosephosphate isomerase (2 entities in total)
• 機能のキーワード: tim-barrel, triosephosphate isomerase, isomerase
• 由来する生物種: Opisthorchis viverrini
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 118940.38

構造登録者

Son, J.,Kim, S.,Kim, S.E.,Lee, H.,Lee, M.R.,Hwang, K.Y. (登録日: 2018-03-07, 公開日: 2018-10-24, 最終更新日: 2023-11-22)

主引用文献

Son, J.,Kim, S.,Kim, S.E.,Lee, H.,Lee, M.R.,Hwang, K.Y.
Structural Analysis of an Epitope Candidate of Triosephosphate Isomerase in Opisthorchis viverrini.
Sci Rep, 8:15075-15075, 2018

PubMed Abstract: 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 3-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.

PubMed: 30305716
DOI: 10.1038/s41598-018-33479-8

実験手法

X-RAY DIFFRACTION (1.746 Å)