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==Crystal structure of csal_2705, a putative hydroxyproline epimerase from CHROMOHALOBACTER SALEXIGENS (TARGET EFI-506486), SPACE GROUP P212121, unliganded==
==Crystal structure of csal_2705, a putative hydroxyproline epimerase from CHROMOHALOBACTER SALEXIGENS (TARGET EFI-506486), SPACE GROUP P212121, unliganded==
<StructureSection load='4jci' size='340' side='right' caption='[[4jci]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='4jci' size='340' side='right'caption='[[4jci]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4jci]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chromohalobacter_salexigens_dsm_3043 Chromohalobacter salexigens dsm 3043]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JCI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JCI FirstGlance]. <br>
<table><tr><td colspan='2'>[[4jci]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chromohalobacter_salexigens_DSM_3043 Chromohalobacter salexigens DSM 3043]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JCI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.7&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Csal_2705 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=290398 Chromohalobacter salexigens DSM 3043])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=4jci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jci OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jci RCSB], [http://www.ebi.ac.uk/pdbsum/4jci PDBsum]</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=4jci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jci OCA], [https://pdbe.org/4jci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jci RCSB], [https://www.ebi.ac.uk/pdbsum/4jci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jci ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/4HYPE_CHRSD 4HYPE_CHRSD] 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. Displays no proline racemase activity.<ref>PMID:24980702</ref>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chromohalobacter salexigens dsm 3043]]
[[Category: Chromohalobacter salexigens DSM 3043]]
[[Category: Almo, S C]]
[[Category: Large Structures]]
[[Category: Bhosle, R]]
[[Category: Al Obaidi NF]]
[[Category: Chowdhury, S]]
[[Category: Almo SC]]
[[Category: Efi]]
[[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: Enzyme function initiative]]
[[Category: Isomerase]]
[[Category: Putative hydroxyproline epimerase]]
[[Category: Structural genomic]]

Latest revision as of 18:40, 20 September 2023

Crystal structure of csal_2705, a putative hydroxyproline epimerase from CHROMOHALOBACTER SALEXIGENS (TARGET EFI-506486), SPACE GROUP P212121, unligandedCrystal structure of csal_2705, a putative hydroxyproline epimerase from CHROMOHALOBACTER SALEXIGENS (TARGET EFI-506486), SPACE GROUP P212121, unliganded

Structural highlights

4jci is a 2 chain structure with sequence from Chromohalobacter salexigens DSM 3043. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

4HYPE_CHRSD 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. 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

4jci, resolution 1.70Å

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