1jpm
From Proteopedia
(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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| - | [[Image:1jpm.jpg|left|200px]]<br /><applet load="1jpm" size=" | + | [[Image:1jpm.jpg|left|200px]]<br /><applet load="1jpm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jpm, resolution 2.25Å" /> | caption="1jpm, resolution 2.25Å" /> | ||
'''L-Ala-D/L-Glu Epimerase'''<br /> | '''L-Ala-D/L-Glu Epimerase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The members of the enolase superfamily catalyze different overall | + | 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== | ==About this Structure== | ||
| - | 1JPM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1JPM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JPM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gerlt, J | + | [[Category: Gerlt, J A.]] |
| - | [[Category: Gulick, A | + | [[Category: Gulick, A M.]] |
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
| - | [[Category: Schmidt, D | + | [[Category: Schmidt, D M.Z.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: muconate lactonizing subgroup]] | [[Category: muconate lactonizing subgroup]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:15 2008'' |
Revision as of 11:25, 21 February 2008
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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 and 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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