1hfw

From Proteopedia

Revision as of 11:44, 30 October 2007

X-RAY STRUCTURE OF THE COMPLEX BETWEEN ERWINIA CHRYSANTHEMI L-ASPARAGINASE AND L-GLUTAMATE

Overview

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 Structure

1HFW is a [Single protein] structure of sequence from [Erwinia chrysanthemi] with GLU 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].

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:11341830

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