5TVD
Crystal structure of Tm16
Summary for 5TVD
| Entry DOI | 10.2210/pdb5tvd/pdb |
| Descriptor | Tm16 (2 entities in total) |
| Functional Keywords | phosphatidylethanolamine-binding protein, unknown function |
| Biological source | Trichuris muris (Mouse whipworm) |
| Total number of polymer chains | 1 |
| Total formula weight | 21371.85 |
| Authors | Asojo, O.A. (deposition date: 2016-11-08, release date: 2017-08-30, Last modification date: 2023-10-04) |
| Primary citation | Liu, Z.,Kelleher, A.,Tabb, S.,Wei, J.,Pollet, J.,Hotez, P.J.,Bottazzi, M.E.,Zhan, B.,Asojo, O.A. Identification, Characterization, and Structure of Tm16 from Trichuris muris. J Parasitol Res, 2017:4342789-4342789, 2017 Cited by PubMed Abstract: Trichuriasis is a disease of poverty for which excretory and secretory (ES) products that induce the protective immunity are being investigated as candidate vaccines antigens. In this study, ES products of and immune sera were produced. The immune sera recognized more than 20 proteins on a 2D-gel of ES products of adult worms. Tm16 was one of the proteins identified by mass spectrometry. Tm16 shares 57% sequence identity with Ov16, an immunodominant diagnostic antigen from . Recombinant Tm16 with a carboxyl terminal hexahistidine was produced using Polyclonal antibodies against rTm16 were generated by one-prime and two-boost immunization of three female Balb/c mice with 25 g of recombinant Tm16 emulsified with ISA720 adjuvant. These polyclonal antibodies confirmed that Tm16 is localized to the ES products and the soluble fraction of the adult worm. Additionally, the high-resolution crystal structure of Tm16 was solved by molecular replacement. Tm16 belongs to the phosphatidylethanolamine-binding-like protein (PEBP1) family and this is the first structure of a PEBP1 from a parasite. PubMed: 28884022DOI: 10.1155/2017/4342789 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.734 Å) |
Structure validation
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