3ECA

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

Summary for 3ECA

• Entry DOI: 10.2210/pdb3eca/pdb
• Descriptor: L-asparaginase 2, ASPARTIC ACID (3 entities in total)
• Functional Keywords: hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 139039.48

Authors

Swain, A.L.,Jaskolski, M.,Housset, D.,Rao, J.K.M.,Wlodawer, A. (deposition date: 1993-07-02, release date: 1993-10-31, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)