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PDBsum entry 3eca
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of escherichia coli l-Asparaginase, An enzyme used in cancer therapy.
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Authors
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A.L.Swain,
M.Jaskólski,
D.Housset,
J.K.Rao,
A.Wlodawer.
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Ref.
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Proc Natl Acad Sci U S A, 1993,
90,
1474-1478.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Preliminary crystal structure of acinetobacter glutaminasificans glutaminase-Asparaginase.
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Authors
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H.L.Ammon,
I.T.Weber,
A.Wlodawer,
R.W.Harrison,
G.L.Gilliland,
K.C.Murphy,
L.Sjölin,
J.Roberts.
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Ref.
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J Biol Chem, 1988,
263,
150-156.
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PubMed id
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