8UHV
X-ray crystal structure of Toxoplasma gondii Apo GalNAc-T3
Summary for 8UHV
| Entry DOI | 10.2210/pdb8uhv/pdb |
| Descriptor | Glycosyl transferase, GLYCEROL, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
| Functional Keywords | gt-a fold galnac glycosyltransferase, mucin-type o-glycosylation, toxoplasma gondii cyst wall glycosylation, transferase |
| Biological source | Toxoplasma gondii ME49 |
| Total number of polymer chains | 1 |
| Total formula weight | 64371.03 |
| Authors | Kumar, P.,Samara, N.L. (deposition date: 2023-10-09, release date: 2024-05-15, Last modification date: 2024-10-23) |
| Primary citation | Kumar, P.,Tomita, T.,Gerken, T.A.,Ballard, C.J.,Lee, Y.S.,Weiss, L.M.,Samara, N.L. A Toxoplasma gondii O-glycosyltransferase that modulates bradyzoite cyst wall rigidity is distinct from host homologues. Nat Commun, 15:3792-3792, 2024 Cited by PubMed Abstract: Infection with the apicomplexan protozoan Toxoplasma gondii can be life-threatening in immunocompromised hosts. Transmission frequently occurs through the oral ingestion of T. gondii bradyzoite cysts, which transition to tachyzoites, disseminate, and then form cysts containing bradyzoites in the central nervous system, resulting in latent infection. Encapsulation of bradyzoites by a cyst wall is critical for immune evasion, survival, and transmission. O-glycosylation of the protein CST1 by the mucin-type O-glycosyltransferase T. gondii (Txg) GalNAc-T3 influences cyst wall rigidity and stability. Here, we report X-ray crystal structures of TxgGalNAc-T3, revealing multiple features that are strictly conserved among its apicomplexan homologues. This includes a unique 2 metal that is coupled to substrate binding and enzymatic activity in vitro and cyst wall O-glycosylation in T. gondii. The study illustrates the divergence of pathogenic protozoan GalNAc-Ts from their host homologues and lays the groundwork for studying apicomplexan GalNAc-Ts as therapeutic targets in disease. PubMed: 38710711DOI: 10.1038/s41467-024-48253-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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