4OSY

STRUCTURE of FULLY-CLEAVED GLYCINE-BOUND HUMAN L-ASPARAGINASE PROTEIN

「4HLP」から置き換えられました

4OSY の概要

• エントリーDOI: 10.2210/pdb4osy/pdb
• 関連するPDBエントリー: 4OSX
• 分子名称: Isoaspartyl peptidase/L-asparaginase, SODIUM ION, GLYCINE, ... (4 entities in total)
• 機能のキーワード: ntn enzyme, hydrolase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64811.53

構造登録者

Nomme, J.,Lavie, A. (登録日: 2014-02-13, 公開日: 2014-03-05, 最終更新日: 2023-09-20)

主引用文献

Su, Y.,Karamitros, C.S.,Nomme, J.,McSorley, T.,Konrad, M.,Lavie, A.
Free glycine accelerates the autoproteolytic activation of human asparaginase.
Chem.Biol., 20:533-540, 2013

PubMed Abstract: Human asparaginase 3 (hASNase3), which belongs to the N-terminal nucleophile hydrolase superfamily, is synthesized as a single polypeptide that is devoid of asparaginase activity. Intramolecular autoproteolytic processing releases the amino group of Thr168, a moiety required for catalyzing asparagine hydrolysis. Recombinant hASNase3 purifies as the uncleaved, asparaginase-inactive form and undergoes self-cleavage to the active form at a very slow rate. Here, we show that the free amino acid glycine selectively acts to accelerate hASNase3 cleavage both in vitro and in human cells. Other small amino acids such as alanine, serine, or the substrate asparagine are not capable of promoting autoproteolysis. Crystal structures of hASNase3 in complex with glycine in the uncleaved and cleaved enzyme states reveal the mechanism of glycine-accelerated posttranslational processing and explain why no other amino acid can substitute for glycine.

PubMed: 23601642
DOI: 10.1016/j.chembiol.2013.03.006

実験手法

X-RAY DIFFRACTION (1.91 Å)