1jpm
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(New page: 200px<br /><applet load="1jpm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jpm, resolution 2.25Å" /> '''L-Ala-D/L-Glu Epimer...)
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Revision as of 21:54, 24 November 2007
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L-Ala-D/L-Glu Epimerase
Overview
The members of the enolase superfamily catalyze different overall, reactions, yet share a partial reaction that involves Mg(2+)-assisted, enolization of the substrate carboxylate anion. The fate of the resulting, enolate intermediate is determined by the active site of each enzyme., Several members of this superfamily have been structurally characterized, to permit an understanding of the evolutionary strategy for using a common, structural motif to catalyze different overall reactions. In the preceding, paper, two new members of the superfamily were identified that catalyze, the epimerization of the glutamate residue in L-Ala-D/L-Glu. These enzymes, belong to the muconate lactonizing enzyme subgroup of the enolase, superfamily, and their sequences are only 31% identical. The structure of, YcjG, the epimerase from Escherichia coli, was determined by MAD phasing, using both the SeMet-labeled protein and a heavy atom derivative. The, structure of YkfB, the epimerase from Bacillus subtilis, was determined by, molecular replacement using the muconate lactonizing enzyme as a search, model. In this paper, we report the three-dimensional structures of these, enzymes and compare them to the structure of o-succinylbenzoate synthase, another member of the muconate lactonizing enzyme subgroup.
About this Structure
1JPM is a Single protein structure of sequence from Bacillus subtilis with MG and GOL as ligands. Full crystallographic information is available from OCA.
Reference
Evolution of enzymatic activities in the enolase superfamily: crystal structures of the L-Ala-D/L-Glu epimerases from Escherichia coli and Bacillus subtilis., Gulick AM, Schmidt DM, Gerlt JA, Rayment I, Biochemistry. 2001 Dec 25;40(51):15716-24. PMID:11747448
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