6E4R

Crystal Structure of the Drosophila Melanogaster Polypeptide N-Acetylgalactosaminyl Transferase PGANT9B

6E4R の概要

• エントリーDOI: 10.2210/pdb6e4r/pdb
• 分子名称: polypeptide N-acetylgalactosaminyltransferase 9, 2-acetamido-2-deoxy-beta-D-glucopyranose, 1,2-ETHANEDIOL, ... (6 entities in total)
• 機能のキーワード: o-glycosyltransferase, gt-a fold catalytic domain, ricin b-type lectin domain, metal-dependent enzyme, transferase
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 117636.09

構造登録者

Samara, N.L.,Tabak, L.A.,Ten Hagen, K.G. (登録日: 2018-07-18, 公開日: 2018-09-12, 最終更新日: 2024-11-06)

主引用文献

Ji, S.,Samara, N.L.,Revoredo, L.,Zhang, L.,Tran, D.T.,Muirhead, K.,Tabak, L.A.,Ten Hagen, K.G.
A molecular switch orchestrates enzyme specificity and secretory granule morphology.
Nat Commun, 9:3508-3508, 2018

PubMed Abstract: Regulated secretion is an essential process where molecules destined for export are directed to membranous secretory granules, where they undergo packaging and maturation. Here, we identify a gene (pgant9) that influences the structure and shape of secretory granules within the Drosophila salivary gland. Loss of pgant9, which encodes an O-glycosyltransferase, results in secretory granules with an irregular, shard-like morphology, and altered glycosylation of cargo. Interestingly, pgant9 undergoes a splicing event that acts as a molecular switch to alter the charge of a loop controlling access to the active site of the enzyme. The splice variant with the negatively charged loop glycosylates the positively charged secretory cargo and rescues secretory granule morphology. Our study highlights a mechanism for dictating substrate specificity within the O-glycosyltransferase enzyme family. Moreover, our in vitro and in vivo studies suggest that the glycosylation status of secretory cargo influences the morphology of maturing secretory granules.

PubMed: 30158631
DOI: 10.1038/s41467-018-05978-9

実験手法

X-RAY DIFFRACTION (2.061 Å)