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 2.4&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:3eca.gif|left|200px]]<br /><applet load="3eca" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:3eca.gif|left|200px]]<br /><applet load="3eca" size="350" color="white" frame="true" align="right" spinBox="true"
caption="3eca, resolution 2.4&Aring;" />
caption="3eca, resolution 2.4&Aring;" />
'''CRYSTAL STRUCTURE OF ESCHERICHIA COLI L-ASPARAGINASE, AN ENZYME USED IN CANCER THERAPY'''<br />
'''CRYSTAL STRUCTURE OF ESCHERICHIA COLI L-ASPARAGINASE, AN ENZYME USED IN CANCER THERAPY'''<br />
==Overview==
==Overview==
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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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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==
==About this Structure==
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3ECA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ASP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3ECA OCA].
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3ECA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ASP:'>ASP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ECA OCA].
==Reference==
==Reference==
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[[Category: Housset, D.]]
[[Category: Housset, D.]]
[[Category: Jaskolski, M.]]
[[Category: Jaskolski, M.]]
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[[Category: Rao, J.K.M.]]
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[[Category: Rao, J K.M.]]
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[[Category: Swain, A.L.]]
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[[Category: Swain, A L.]]
[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
[[Category: ASP]]
[[Category: ASP]]
[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:40:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:09:06 2008''

Revision as of 17:09, 21 February 2008


3eca, resolution 2.4Å

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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 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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