8UI6
X-ray crystal structure of Toxoplasma gondii GalNAc-T3 in complex with UDP-GalNAc, Mn2+, and Muc5AC-3,13
8UI6 の概要
エントリーDOI | 10.2210/pdb8ui6/pdb |
分子名称 | Glycosyl transferase, Mucin-5AC, MANGANESE (II) ION, ... (7 entities in total) |
機能のキーワード | gt-a fold galnac glycosyltransferase, mucin-type o-glycosylation, toxoplasma gondii cyst wall glycosylation, transferase |
由来する生物種 | Toxoplasma gondii ME49 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 65945.19 |
構造登録者 | |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.65 Å) |
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