1hg0: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
1HG0 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]] with SIN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ | 1HG0 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]] with SIN 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]]. Structure known Active Sites: AS1, AS2, AS3, AS4, LI1, LI2, LI3 and LI4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HG0 OCA]]. | ||
==Reference== | ==Reference== | ||
Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase., Aghaiypour K, Wlodawer A, Lubkowski J, Biochemistry. 2001 May 15;40(19):5655-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11341830 11341830] | Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase., Aghaiypour K, Wlodawer A, Lubkowski J, Biochemistry. 2001 May 15;40(19):5655-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11341830 11341830] | ||
[[Category: Asparaginase]] | |||
[[Category: Erwinia chrysanthemi]] | [[Category: Erwinia chrysanthemi]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: x-ray]] | [[Category: x-ray]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:25:40 2007'' | ||
Revision as of 11:20, 30 October 2007
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X-RAY STRUCTURE OF THE COMPLEX BETWEEN ERWINIA CHRYSANTHEMI L-ASPARAGINASE AND SUCCINIC ACID
OverviewOverview
Bacterial L-asparaginases, enzymes that catalyze the hydrolysis of, L-asparagine to aspartic acid, have been used for over 30 years as, therapeutic agents in the treatment of acute childhood lymphoblastic, leukemia. Other substrates of asparaginases include L-glutamine, D-asparagine, and succinic acid monoamide. In this report, we present, high-resolution crystal structures of the complexes of Erwinia, chrysanthemi L-asparaginase (ErA) with the products of such reactions that, also can serve as substrates, namely L-glutamic acid (L-Glu), D-aspartic, acid (D-Asp), and succinic acid (Suc). Comparison of the four independent, active sites within each complex indicates unique and specific binding of, the ligand molecules; the mode of binding is also similar between, complexes. The lack of the ... [(full description)]
About this StructureAbout this Structure
1HG0 is a [Single protein] structure of sequence from [Erwinia chrysanthemi] with SIN as [ligand]. Active as [Asparaginase], with EC number [3.5.1.1]. Structure known Active Sites: AS1, AS2, AS3, AS4, LI1, LI2, LI3 and LI4. Full crystallographic information is available from [OCA].
ReferenceReference
Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase., Aghaiypour K, Wlodawer A, Lubkowski J, Biochemistry. 2001 May 15;40(19):5655-64. PMID:11341830
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