Crystal structure of epidermal growth factor domain-specific O-linked N-acetylglucosamine transferase reveals a conserved N–R–R constellation for uridine diphosphate recognition in the GT61 family
Yuko Tashima, Masamichi Nagae, Jiaoyang Jiang, Tetsuya Okajima · 2026
Read Crystal structure of epidermal growth factor domain-specific O-linked N-acetylglucosamine transferase reveals a conserved N–R–R constellation for uridine diphosphate recognition in the GT61 family by Yuko Tashima, Masamichi Nagae, Jiaoyang Jiang, Tetsuya Okajima (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13123520.txt.
Description
Yuko Tashima, Masamichi Nagae, Jiaoyang Jiang, and Tetsuya Okajima solve the structure of an enzyme that tags proteins with sugar, in a 2026 study. The enzyme works inside the cell's folding compartment. It attaches a single sugar unit to a class of protein domains. The team froze the enzyme with its sugar donor bound. X-ray crystallography revealed the pair's shape. Key contact points were then tested by mutation.
Three residues form a signature grip on the donor. One is an asparagine and two are arginines. The grip needs no metal ions, breaking a common pattern. The same trio appears in a close enzyme relative. It is conserved across animals and green plants. That spread suggests an ancient shared mechanism. The structure helps explain disease-linked mutations in the enzyme. It also frames how this enzyme family evolved. Sugar-tagging enzymes matter for protein quality control across life.
Catalog record
| CREATOR | Yuko Tashima, Masamichi Nagae, Jiaoyang Jiang, Tetsuya Okajima |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 33 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |