3ECA

CRYSTAL STRUCTURE OF ESCHERICHIA COLI L-ASPARAGINASE, AN ENZYME USED IN CANCER THERAPY (ELSPAR)

3ECA の概要

• エントリーDOI: 10.2210/pdb3eca/pdb
• 分子名称: L-asparaginase 2, ASPARTIC ACID (3 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 139039.48

構造登録者

Swain, A.L.,Jaskolski, M.,Housset, D.,Rao, J.K.M.,Wlodawer, A. (登録日: 1993-07-02, 公開日: 1993-10-31, 最終更新日: 2024-10-09)

主引用文献

Swain, A.L.,Jaskolski, M.,Housset, D.,Rao, J.K.,Wlodawer, A.
Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy.
Proc.Natl.Acad.Sci.USA, 90:1474-1478, 1993

PubMed Abstract: The crystal structure of Escherichia coli asparaginase II (EC 3.5.1.1), a drug (Elspar) used for the treatment of acute lymphoblastic leukemia, has been determined at 2.3 A resolution by using data from a single heavy atom derivative in combination with molecular replacement. The atomic model was refined to an R factor of 0.143. This enzyme, active as a homotetramer with 222 symmetry, belongs to the class of alpha/beta proteins. Each subunit has two domains with unique topological features. On the basis of present structural evidence consistent with previous biochemical studies, we propose locations for the active sites between the N- and C-terminal domains belonging to different subunits and postulate a catalytic role for Thr-89.

PubMed: 8434007
DOI: 10.1073/pnas.90.4.1474

実験手法

X-RAY DIFFRACTION (2.4 Å)