4h2h: Difference between revisions

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==Crystal structure of an enolase (mandalate racemase subgroup, target EFI-502101) from Pelagibaca bermudensis htcc2601, with bound mg and l-4-hydroxyproline betaine (betonicine)==
==Crystal structure of an enolase (mandalate racemase subgroup, target EFI-502101) from Pelagibaca bermudensis htcc2601, with bound mg and l-4-hydroxyproline betaine (betonicine)==
<StructureSection load='4h2h' size='340' side='right' caption='[[4h2h]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='4h2h' size='340' side='right'caption='[[4h2h]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4h2h]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Pelbh Pelbh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H2H FirstGlance]. <br>
<table><tr><td colspan='2'>[[4h2h]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Salipiger_bermudensis_HTCC2601 Salipiger bermudensis HTCC2601]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H2H FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0XW:(2S,4R)-4-HYDROXY-1,1-DIMETHYLPYRROLIDINIUM-2-CARBOXYLATE'>0XW</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0XW:(2S,4R)-4-HYDROXY-1,1-DIMETHYLPYRROLIDINIUM-2-CARBOXYLATE'>0XW</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pmq|2pmq]]</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=4h2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h2h OCA], [https://pdbe.org/4h2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h2h RCSB], [https://www.ebi.ac.uk/pdbsum/4h2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h2h ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">R2601_01638 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=314265 PELBH])</td></tr>
<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=4h2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h2h OCA], [http://pdbe.org/4h2h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h2h RCSB], [http://www.ebi.ac.uk/pdbsum/4h2h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h2h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HPBD_SALBH HPBD_SALBH] 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. To a lesser extent, can also catalyze the racemization of L-proline betaine.<ref>PMID:24056934</ref>
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4h2h" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4h2h" style="background-color:#fffaf0;"></div>
==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: Pelbh]]
[[Category: Large Structures]]
[[Category: Almo, S C]]
[[Category: Salipiger bermudensis HTCC2601]]
[[Category: EFI, Enzyme Function Initiative]]
[[Category: Almo SC]]
[[Category: Gerlt, J A]]
[[Category: Gerlt JA]]
[[Category: Imker, H J]]
[[Category: Imker HJ]]
[[Category: Morisco, L L]]
[[Category: Morisco LL]]
[[Category: Sojitra, S]]
[[Category: Sojitra S]]
[[Category: Vetting, M W]]
[[Category: Vetting MW]]
[[Category: Wasserman, S R]]
[[Category: Wasserman SR]]
[[Category: Efi]]
[[Category: Enolase]]
[[Category: Enzyme function initiative]]
[[Category: Isomerase]]
[[Category: Mandelate racemase subgroup]]
[[Category: Structural genomic]]

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