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Purification, crystallization and preliminary X-ray analysis of aspartokinase III from Escherichia coli.

作者信息

Blanco Julio, Viola Ronald E

机构信息

Department of Chemistry, University of Toledo, 2801 West Bancroft Street, Toledo, Ohio 43606, USA.

出版信息

Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):352-4. doi: 10.1107/s0907444901020728. Epub 2002 Jan 24.

DOI:10.1107/s0907444901020728
PMID:11807275
Abstract

Aspartokinase III catalyzes the commitment step in the aspartate metabolism pathway, the phosphorylation of aspartic acid. The Escherichia coli enzyme has been crystallized in the presence of its natural substrate (aspartic acid) and Mg-ADP and diffraction data has been collected at a synchroton source. The crystals belong to the orthorhombic space group C222(1), with unit-cell parameters a = 60.44, b = 190.31, c = 99.55 A, and data 99.3% complete to 2.7 A. Solving the structure of AK III will provide the first structure of an aspartokinase from any organism.

摘要

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