7S69

N-acetylglucosamine-1-phosphotransferase (GNPT) gamma subunit (GNPTG), from clawed frog

7S69 の概要

• エントリーDOI: 10.2210/pdb7s69/pdb
• 分子名称: N-acetylglucosamine-1-phosphotransferase gamma subunit, alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: gnpt, mannose, mannose 6-phosphate receptor homology (mrh) domain, mucolipidosis, sugar binding protein
• 由来する生物種: Xenopus laevis (African clawed frog)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69811.79

構造登録者

Gorelik, A.,Illes, K.,Nagar, B. (登録日: 2021-09-13, 公開日: 2022-05-25, 最終更新日: 2024-10-09)

主引用文献

Gorelik, A.,Illes, K.,Bui, K.H.,Nagar, B.
Structures of the mannose-6-phosphate pathway enzyme, GlcNAc-1-phosphotransferase.
Proc.Natl.Acad.Sci.USA, 119:e2203518119-e2203518119, 2022

PubMed Abstract: The mannose-6-phosphate (M6P) pathway is responsible for the transport of hydrolytic enzymes to lysosomes. N-acetylglucosamine-1-phosphotransferase (GNPT) catalyzes the first step of tagging these hydrolases with M6P, which when recognized by receptors in the Golgi diverts them to lysosomes. Genetic defects in the GNPT subunits, GNPTAB and GNPTG, cause the lysosomal storage diseases mucolipidosis types II and III. To better understand its function, we determined partial three-dimensional structures of the GNPT complex. The catalytic domain contains a deep cavity for binding of uridine diphosphate--acetylglucosamine, and the surrounding residues point to a one-step transfer mechanism. An isolated structure of the gamma subunit of GNPT reveals that it can bind to mannose-containing glycans in different configurations, suggesting that it may play a role in directing glycans into the active site. These findings may facilitate the development of therapies for lysosomal storage diseases.

PubMed: 35939698
DOI: 10.1073/pnas.2203518119

実験手法

X-RAY DIFFRACTION (3.04 Å)