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 2.25&Aring;" /> '''L-Ala-D/L-Glu Epimer...)
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[[Image:1jpm.jpg|left|200px]]<br /><applet load="1jpm" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jpm, resolution 2.25&Aring;" />
 
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'''L-Ala-D/L-Glu Epimerase'''<br />
 
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==Overview==
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==L-Ala-D/L-Glu Epimerase==
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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.
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<StructureSection load='1jpm' size='340' side='right'caption='[[1jpm]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1jpm]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JPM FirstGlance]. <br>
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JPM OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jpm OCA], [https://pdbe.org/1jpm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jpm RCSB], [https://www.ebi.ac.uk/pdbsum/1jpm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jpm ProSAT]</span></td></tr>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11747448 11747448]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AEEP_BACSU AEEP_BACSU] Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-Glu and has probably a role in the metabolism of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the reverse reaction and the epimerization of the other Ala-X dipeptides L-Ala-L-Asp, L-Ala-L-Leu, L-Ala-L-Met, and L-Ala-L-Ser. Is not able to epimerize other L-Ala-X dipeptides. Is also active with L-Ser-L-Glu and, oddly, L-Pro-L-Glu, but not with L-Glu-L-Glu, L-Lys-L-Glu, L-Lys-L-Ala, or D-Ala-D-Ala.<ref>PMID:11747447</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jp/1jpm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jpm ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Gerlt, J.A.]]
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[[Category: Gerlt JA]]
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[[Category: Gulick, A.M.]]
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[[Category: Gulick AM]]
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[[Category: Rayment, I.]]
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[[Category: Rayment I]]
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[[Category: Schmidt, D.M.Z.]]
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[[Category: Schmidt DMZ]]
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[[Category: GOL]]
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[[Category: MG]]
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[[Category: alpha-beta barrel]]
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[[Category: enolase superfamily]]
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[[Category: muconate lactonizing subgroup]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:01:53 2007''
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Current revision

L-Ala-D/L-Glu Epimerase

PDB ID 1jpm

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