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==Crystal structure of an enolase (mandelate racemase subgroup) from paracococus denitrificans pd1222 (target nysgrc-012907) with bound l-proline betaine (substrate)== | ==Crystal structure of an enolase (mandelate racemase subgroup) from paracococus denitrificans pd1222 (target nysgrc-012907) with bound l-proline betaine (substrate)== | ||
<StructureSection load='4j1o' size='340' side='right' caption='[[4j1o]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='4j1o' size='340' side='right'caption='[[4j1o]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4j1o]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4j1o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans_PD1222 Paracoccus denitrificans PD1222]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J1O FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PBE:1,1-DIMETHYL-PROLINIUM'>PBE</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PBE:1,1-DIMETHYL-PROLINIUM'>PBE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4j1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j1o OCA], [https://pdbe.org/4j1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j1o RCSB], [https://www.ebi.ac.uk/pdbsum/4j1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j1o ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/HPBD_PARDP HPBD_PARDP] Catalyzes the 2-epimerization of trans-4-hydroxy-L-proline betaine (tHyp-B) to cis-4-hydroxy-D-proline betaine (cHyp-B). Is involved in a catabolic pathway that degrades tHyp-B to alpha-ketoglutarate. This pathway would permit the utilization of tHyp-B as a carbon and nitrogen source in the absence of osmotic stress, since tHyp-B functions as an osmolyte and is not catabolized when it is needed as osmoprotectant. Can also catalyze the racemization of L-proline betaine.<ref>PMID:24056934</ref> | ||
==See Also== | |||
*[[Mandelate racemase/muconate lactonizing enzyme 3D structures|Mandelate racemase/muconate lactonizing enzyme 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Paracoccus denitrificans | [[Category: Large Structures]] | ||
[[Category: Almo | [[Category: Paracoccus denitrificans PD1222]] | ||
[[Category: Bhosle | [[Category: Almo SC]] | ||
[[Category: Bonanno | [[Category: Bhosle R]] | ||
[[Category: Chamala | [[Category: Bonanno JB]] | ||
[[Category: Evans | [[Category: Chamala S]] | ||
[[Category: Gerlt | [[Category: Evans B]] | ||
[[Category: Gizzi | [[Category: Gerlt JA]] | ||
[[Category: Hammonds | [[Category: Gizzi A]] | ||
[[Category: Hillerich | [[Category: Hammonds J]] | ||
[[Category: Kar | [[Category: Hillerich B]] | ||
[[Category: LaFleur | [[Category: Kar A]] | ||
[[Category: Love | [[Category: LaFleur J]] | ||
[[Category: Morisco | [[Category: Love J]] | ||
[[Category: Morisco LL]] | |||
[[Category: Seidel | [[Category: Seidel RD]] | ||
[[Category: Sojitra | [[Category: Sojitra S]] | ||
[[Category: Stead | [[Category: Stead M]] | ||
[[Category: Toro | [[Category: Toro R]] | ||
[[Category: Vetting | [[Category: Vetting MW]] | ||
[[Category: Villigas | [[Category: Villigas G]] | ||
[[Category: Wasserman | [[Category: Wasserman SR]] | ||
Latest revision as of 15:00, 1 March 2024
Crystal structure of an enolase (mandelate racemase subgroup) from paracococus denitrificans pd1222 (target nysgrc-012907) with bound l-proline betaine (substrate)Crystal structure of an enolase (mandelate racemase subgroup) from paracococus denitrificans pd1222 (target nysgrc-012907) with bound l-proline betaine (substrate)
Structural highlights
FunctionHPBD_PARDP Catalyzes the 2-epimerization of trans-4-hydroxy-L-proline betaine (tHyp-B) to cis-4-hydroxy-D-proline betaine (cHyp-B). Is involved in a catabolic pathway that degrades tHyp-B to alpha-ketoglutarate. This pathway would permit the utilization of tHyp-B as a carbon and nitrogen source in the absence of osmotic stress, since tHyp-B functions as an osmolyte and is not catabolized when it is needed as osmoprotectant. Can also catalyze the racemization of L-proline betaine.[1] See AlsoReferences
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