5ZG4

Crystal Structure of Triosephosphate isomerase SAD deletion mutant from Opisthorchis viverrini

Summary for 5ZG4

• Entry DOI: 10.2210/pdb5zg4/pdb
• Related: 5ZFX
• Descriptor: Triosephosphate isomerase (2 entities in total)
• Functional Keywords: tim-barrel, triosephosphate isomerase, isomerase
• Biological source: Opisthorchis viverrini
• Total number of polymer chains: 4
• Total formula weight: 118940.38

Authors

Son, J.,Kim, S.,Kim, S.E.,Lee, H.,Lee, M.R.,Hwang, K.Y. (deposition date: 2018-03-07, release date: 2018-10-24, Last modification date: 2023-11-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.746 Å)