6E7I

Human ppGalNAcT2 I253A/L310A Mutant with EA2 and UDP

6E7I の概要

• エントリーDOI: 10.2210/pdb6e7i/pdb
• 分子名称: Polypeptide N-acetylgalactosaminyltransferase 2, EA2, URIDINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: glycosyltransferase, glycosylation, bump-hole, galnac, transferase
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62447.64

構造登録者

Bertozzi, C.R.,Schumann, B.,Agbay, A.J. (登録日: 2018-07-26, 公開日: 2020-01-29, 最終更新日: 2024-10-16)

主引用文献

Schumann, B.,Malaker, S.A.,Wisnovsky, S.P.,Debets, M.F.,Agbay, A.J.,Fernandez, D.,Wagner, L.J.S.,Lin, L.,Li, Z.,Choi, J.,Fox, D.M.,Peh, J.,Gray, M.A.,Pedram, K.,Kohler, J.J.,Mrksich, M.,Bertozzi, C.R.
Bump-and-Hole Engineering Identifies Specific Substrates of Glycosyltransferases in Living Cells.
Mol.Cell, 78:824-834.e15, 2020

PubMed Abstract: Studying posttranslational modifications classically relies on experimental strategies that oversimplify the complex biosynthetic machineries of living cells. Protein glycosylation contributes to essential biological processes, but correlating glycan structure, underlying protein, and disease-relevant biosynthetic regulation is currently elusive. Here, we engineer living cells to tag glycans with editable chemical functionalities while providing information on biosynthesis, physiological context, and glycan fine structure. We introduce a non-natural substrate biosynthetic pathway and use engineered glycosyltransferases to incorporate chemically tagged sugars into the cell surface glycome of the living cell. We apply the strategy to a particularly redundant yet disease-relevant human glycosyltransferase family, the polypeptide N-acetylgalactosaminyl transferases. This approach bestows a gain-of-chemical-functionality modification on cells, where the products of individual glycosyltransferases can be selectively characterized or manipulated to understand glycan contribution to major physiological processes.

PubMed: 32325029
DOI: 10.1016/j.molcel.2020.03.030

実験手法

X-RAY DIFFRACTION (1.8 Å)