3eca
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(New page: 200px<br /><applet load="3eca" size="450" color="white" frame="true" align="right" spinBox="true" caption="3eca, resolution 2.4Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 17:32, 20 November 2007
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CRYSTAL STRUCTURE OF ESCHERICHIA COLI L-ASPARAGINASE, AN ENZYME USED IN CANCER THERAPY
Overview
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.
About this Structure
3ECA is a Single protein structure of sequence from Escherichia coli with ASP as ligand. Active as Asparaginase, with EC number 3.5.1.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy., Swain AL, Jaskolski M, Housset D, Rao JK, Wlodawer A, Proc Natl Acad Sci U S A. 1993 Feb 15;90(4):1474-8. PMID:8434007
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