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4mgg

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==Crystal structure of an enolase (mandelate racemase subgroup) from labrenzia aggregata iam 12614 (target nysgrc-012903) with bound mg, space group p212121==
==Crystal structure of an enolase (mandelate racemase subgroup) from labrenzia aggregata iam 12614 (target nysgrc-012903) with bound mg, space group p212121==
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<StructureSection load='4mgg' size='340' side='right' caption='[[4mgg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='4mgg' size='340' side='right'caption='[[4mgg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4mgg]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Labrenzia_aggregata_iam_12614 Labrenzia aggregata iam 12614]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MGG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MGG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4mgg]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Roseibium_aggregatum_IAM_12614 Roseibium aggregatum IAM 12614]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MGG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MGG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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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]] 2.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SIAM614_28497 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=384765 Labrenzia aggregata IAM 12614])</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mgg OCA], [http://pdbe.org/4mgg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mgg RCSB], [http://www.ebi.ac.uk/pdbsum/4mgg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mgg ProSAT]</span></td></tr>
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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=4mgg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mgg OCA], [https://pdbe.org/4mgg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mgg RCSB], [https://www.ebi.ac.uk/pdbsum/4mgg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mgg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/C3HPD_LABAI C3HPD_LABAI]] Catalyzes the dehydration of cis-3-hydroxy-L-proline (c3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Is likely involved in a degradation pathway that converts c3LHyp to L-proline, which allows L.aggregata to grow on c3LHyp as a sole carbon source. Also catalyzes the epimerization of c3LHyp to trans-3-hydroxy-D-proline (t3DHyp), a competing reaction occurring from the same enolate anion intermediate. L-proline, t3LHyp, t4LHyp, c4DHyp and their methylated derivatives are not substrates.<ref>PMID:25608448</ref>
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[https://www.uniprot.org/uniprot/C3HPD_ROSAI C3HPD_ROSAI] Catalyzes the dehydration of cis-3-hydroxy-L-proline (c3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Is likely involved in a degradation pathway that converts c3LHyp to L-proline, which allows L.aggregata to grow on c3LHyp as a sole carbon source. Also catalyzes the epimerization of c3LHyp to trans-3-hydroxy-D-proline (t3DHyp), a competing reaction occurring from the same enolate anion intermediate. L-proline, t3LHyp, t4LHyp, c4DHyp and their methylated derivatives are not substrates.<ref>PMID:25608448</ref>
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==See Also==
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*[[Enolase 3D structures|Enolase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Labrenzia aggregata iam 12614]]
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[[Category: Large Structures]]
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[[Category: Almo, S C]]
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[[Category: Roseibium aggregatum IAM 12614]]
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[[Category: Bonanno, J B]]
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[[Category: Almo SC]]
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[[Category: Gerlt, J A]]
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[[Category: Bonanno JB]]
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[[Category: Morisco, L L]]
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[[Category: Gerlt JA]]
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[[Category: Structural genomic]]
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[[Category: Morisco LL]]
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[[Category: Sojitra, S]]
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[[Category: Sojitra S]]
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[[Category: Vetting, M W]]
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[[Category: Vetting MW]]
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[[Category: Wasserman, S R]]
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[[Category: Wasserman SR]]
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[[Category: Zhang, X]]
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[[Category: Zhang X]]
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[[Category: Enolase]]
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[[Category: Isomerase]]
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[[Category: Nysgrc]]
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Current revision

Crystal structure of an enolase (mandelate racemase subgroup) from labrenzia aggregata iam 12614 (target nysgrc-012903) with bound mg, space group p212121

PDB ID 4mgg

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