1o7j

From Proteopedia

Revision as of 14:47, 18 December 2007

ATOMIC RESOLUTION STRUCTURE OF ERWINIA CHRYSANTHEMI L-ASPARAGINASE

Overview

An X-ray structure of L-asparaginase from Erwinia chrysanthemi (ErA) has, been refined at 1 A resolution to an R factor of below 0.1, using data, collected on a synchrotron source. With four molecules of the enzyme, consisting of 327 amino acids each, this crystal contains one of the, largest asymmetric units of a protein refined to date at atomic, resolution. Previously, structures of ErA and of related enzymes from, other bacterial sources have been refined at resolutions not exceeding 1.7, A; thus, the present structure represents a very significant improvement, in the quality of the available models of these proteins and should, provide a good basis for future studies of the conformational variability, of proteins, identification of subtle conformational features and, corroboration of the stereochemical libraries, amongst other things., L-Asparaginases, which are enzymes that catalyze the hydrolysis of, L-asparagine to aspartic acid, have been used for over 30 y as therapeutic, agents in the treatment of acute childhood lymphoblastic leukemia, although the details of the enzymatic reaction and substrate specificity, have not yet been completely elucidated. This atomic resolution structure, is a step in that direction.

About this Structure

1O7J is a Single protein structure of sequence from Erwinia chrysanthemi with SO4, EDO and GOL as ligands. Active as Asparaginase, with EC number 3.5.1.1 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Atomic resolution structure of Erwinia chrysanthemi L-asparaginase., Lubkowski J, Dauter M, Aghaiypour K, Wlodawer A, Dauter Z, Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):84-92. Epub 2002, Dec 19. PMID:12499544

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