6WG5

Human ectonucleoside triphosphate diphosphohydrolase 4 (ENTPD4, NTPDase 4)

6WG5 の概要

• エントリーDOI: 10.2210/pdb6wg5/pdb
• 分子名称: Ectonucleoside triphosphate diphosphohydrolase 4, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: nucleotide metabolism, glycosylation, askha superfamily, hydrolase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59341.85

構造登録者

Gorelik, A.,Labriola, J.M.,Illes, K.,Nagar, B. (登録日: 2020-04-04, 公開日: 2020-08-12, 最終更新日: 2024-10-23)

主引用文献

Gorelik, A.,Labriola, J.M.,Illes, K.,Nagar, B.
Crystal structure of the nucleotide-metabolizing enzyme NTPDase4.
Protein Sci., 29:2054-2061, 2020

PubMed Abstract: The ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are a family of enzymes found on the cell surface and in the lumen of certain organelles, that are major regulators of purinergic signaling. Their intracellular roles, however, have not been clearly defined. NTPDase4 (UDPase, ENTPD4) is a Golgi protein potentially involved in nucleotide recycling as part of protein glycosylation, and is also found in lysosomes, where its purpose is unknown. To further our understanding of NTPDase4 function, we determined its crystal structure. The enzyme adopts a wide open, inactive conformation. Differences in the nucleotide-binding site relative to its homologs could account for its substrate selectivity. The putative membrane-interacting loop of cell-surface NTPDases is drastically altered in NTPDase4, potentially affecting its interdomain dynamics at the Golgi membrane.

PubMed: 32767432
DOI: 10.1002/pro.3926

実験手法

X-RAY DIFFRACTION (2.6 Å)