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==Crystal structure of a hydroxyproline epimerase from agrobacterium vitis, target efi-506420, with bound trans-4-oh-l-proline==
==Crystal structure of a hydroxyproline epimerase from agrobacterium vitis, target efi-506420, with bound trans-4-oh-l-proline==
<StructureSection load='4lb0' size='340' side='right' caption='[[4lb0]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='4lb0' size='340' side='right'caption='[[4lb0]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4lb0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Agrvs Agrvs]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LB0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LB0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4lb0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_vitis_S4 Agrobacterium vitis S4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LB0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LB0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Avi_0518 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=311402 AGRVS])</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=4lb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lb0 OCA], [https://pdbe.org/4lb0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lb0 RCSB], [https://www.ebi.ac.uk/pdbsum/4lb0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lb0 ProSAT]</span></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=4lb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lb0 OCA], [http://pdbe.org/4lb0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lb0 RCSB], [http://www.ebi.ac.uk/pdbsum/4lb0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lb0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/4HYPE_AGRVS 4HYPE_AGRVS]] Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). May be involved in a degradation pathway of t4LHyp. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp) in vitro. Displays no proline racemase activity.<ref>PMID:24980702</ref>
[https://www.uniprot.org/uniprot/4HYPE_AGRVS 4HYPE_AGRVS] Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). May be involved in a degradation pathway of t4LHyp. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp) in vitro. Displays no proline racemase activity.<ref>PMID:24980702</ref>  
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Agrvs]]
[[Category: Agrobacterium vitis S4]]
[[Category: Almo, S C]]
[[Category: Large Structures]]
[[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 S]]
[[Category: Gerlt JA]]
[[Category: Hammonds, J]]
[[Category: Glenn AS]]
[[Category: Hillerich, B]]
[[Category: Hammonds J]]
[[Category: Imker, H J]]
[[Category: Hillerich B]]
[[Category: Love, J]]
[[Category: Imker HJ]]
[[Category: Morisco, L L]]
[[Category: Love J]]
[[Category: Obaidi, N F.Al]]
[[Category: Morisco LL]]
[[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: Proline racemase family]]
[[Category: Proposed 3-oh and 4-oh proline epimerase]]
[[Category: Structural genomic]]

Revision as of 13:49, 14 December 2022

Crystal structure of a hydroxyproline epimerase from agrobacterium vitis, target efi-506420, with bound trans-4-oh-l-prolineCrystal structure of a hydroxyproline epimerase from agrobacterium vitis, target efi-506420, with bound trans-4-oh-l-proline

Structural highlights

4lb0 is a 2 chain structure with sequence from Agrobacterium vitis S4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

4HYPE_AGRVS Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). May be involved in a degradation pathway of t4LHyp. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp) in vitro. 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

4lb0, resolution 1.70Å

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OCA
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