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==Crystal structure of a putative hydroxyproline epimerase from xanthomonas campestris (TARGET EFI-506516) with bound phosphate and unknown ligand==
==Crystal structure of a putative hydroxyproline epimerase from xanthomonas campestris (TARGET EFI-506516) with bound phosphate and unknown ligand==
<StructureSection load='4juu' size='340' side='right' caption='[[4juu]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='4juu' size='340' side='right'caption='[[4juu]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4juu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Xancp Xancp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JUU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JUU FirstGlance]. <br>
<table><tr><td colspan='2'>[[4juu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris_str._ATCC_33913 Xanthomonas campestris pv. campestris str. ATCC 33913]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JUU FirstGlance]. <br>
</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=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</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]] 1.75&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XCC2415 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=190485 XANCP])</td></tr>
<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=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></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=4juu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4juu OCA], [http://pdbe.org/4juu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4juu RCSB], [http://www.ebi.ac.uk/pdbsum/4juu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4juu ProSAT]</span></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=4juu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4juu OCA], [https://pdbe.org/4juu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4juu RCSB], [https://www.ebi.ac.uk/pdbsum/4juu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4juu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/4HYPE_XANCP 4HYPE_XANCP] Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp), albeit with 500-fold lower efficiency. Displays no proline racemase activity.<ref>PMID:24980702</ref>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Xancp]]
[[Category: Large Structures]]
[[Category: Almo, S C]]
[[Category: Xanthomonas campestris pv. campestris str. ATCC 33913]]
[[Category: Bhosle, R]]
[[Category: Al Obaidi NF]]
[[Category: Chowdhury, S]]
[[Category: Almo SC]]
[[Category: EFI, Enzyme Function Initiative]]
[[Category: Bhosle R]]
[[Category: Evans, B]]
[[Category: Chowdhury S]]
[[Category: Gerlt, J A]]
[[Category: Evans B]]
[[Category: Glenn, A Scott]]
[[Category: Gerlt JA]]
[[Category: Hammonds, J]]
[[Category: Hammonds J]]
[[Category: Hillerich, B]]
[[Category: Hillerich B]]
[[Category: Imker, H J]]
[[Category: Imker HJ]]
[[Category: Love, J]]
[[Category: Love J]]
[[Category: Morisco, L L]]
[[Category: Morisco LL]]
[[Category: Obaidi, N F.Al]]
[[Category: Scott Glenn A]]
[[Category: Seidel, R D]]
[[Category: Seidel RD]]
[[Category: Sojitra, S]]
[[Category: Sojitra S]]
[[Category: Stead, M]]
[[Category: Stead M]]
[[Category: Toro, R]]
[[Category: Toro R]]
[[Category: Vetting, M W]]
[[Category: Vetting MW]]
[[Category: Washington, E]]
[[Category: Washington E]]
[[Category: Wasserman, S R]]
[[Category: Wasserman SR]]
[[Category: Efi]]
[[Category: Enzyme function initiative]]
[[Category: Isomerase]]
[[Category: Structural genomic]]

Latest revision as of 18:49, 20 September 2023

Crystal structure of a putative hydroxyproline epimerase from xanthomonas campestris (TARGET EFI-506516) with bound phosphate and unknown ligandCrystal structure of a putative hydroxyproline epimerase from xanthomonas campestris (TARGET EFI-506516) with bound phosphate and unknown ligand

Structural highlights

4juu is a 2 chain structure with sequence from Xanthomonas campestris pv. campestris str. ATCC 33913. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

4HYPE_XANCP Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp), albeit with 500-fold lower efficiency. Displays no proline racemase activity.[1]

References

  1. Zhao S, Sakai A, Zhang X, Vetting MW, Kumar R, Hillerich B, San Francisco B, Solbiati J, Steves A, Brown S, Akiva E, Barber A, Seidel RD, Babbitt PC, Almo SC, Gerlt JA, Jacobson MP. Prediction and characterization of enzymatic activities guided by sequence similarity and genome neighborhood networks. Elife. 2014 Jun 30;3. doi: 10.7554/eLife.03275. PMID:24980702 doi:http://dx.doi.org/10.7554/eLife.03275

4juu, resolution 1.75Å

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