1jpm
From Proteopedia
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| - | [[Image:1jpm.jpg|left|200px]] | + | [[Image:1jpm.jpg|left|200px]] |
| - | + | ||
| - | '''L-Ala-D/L-Glu Epimerase''' | + | {{Structure |
| + | |PDB= 1jpm |SIZE=350|CAPTION= <scene name='initialview01'>1jpm</scene>, resolution 2.25Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= ykfB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | }} | ||
| + | |||
| + | '''L-Ala-D/L-Glu Epimerase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JPM is a [ | + | 1JPM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JPM OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11747448 11747448] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: muconate lactonizing subgroup]] | [[Category: muconate lactonizing subgroup]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:06:39 2008'' |
Revision as of 10:06, 20 March 2008
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| , resolution 2.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | ykfB (Bacillus subtilis) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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