4jbd: Difference between revisions

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New page: '''Unreleased structure''' The entry 4jbd is ON HOLD Authors: Vetting, M.W., Toro, R., Bhosle, R., Al Obaidi, N.F., Morisco, L.L., Wasserman, S.R., Sojitra, S., Washington, E., Scott Gl...
 
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'''Unreleased structure'''


The entry 4jbd is ON HOLD
==Crystal structure of Pput_1285, a putative hydroxyproline epimerase from Pseudomonas putida f1 (target EFI-506500), open form, space group I2, bound citrate==
<StructureSection load='4jbd' size='340' side='right'caption='[[4jbd]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4jbd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_F1 Pseudomonas putida F1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JBD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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=4jbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jbd OCA], [https://pdbe.org/4jbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jbd RCSB], [https://www.ebi.ac.uk/pdbsum/4jbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jbd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/4HYPE_PSEP1 4HYPE_PSEP1] 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 200-fold lower efficiency.<ref>PMID:24980702</ref>


Authors: Vetting, M.W., Toro, R., Bhosle, R., Al Obaidi, N.F., Morisco, L.L., Wasserman, S.R., Sojitra, S., Washington, E., Scott Glenn, A., Chowdhury, S., Evans, B., Hammonds, J., Stead, M., Hillerich, B., Love, J., Seidel, R.D., Imker, H.J., Gerlt, J.A., Almo, S.C., Enzyme Function Initiative (EFI)
==See Also==
 
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
Description: Crystal structure of pput_1285, a putative hydroxyproline epimerase from pseudomonas putida f1 (target efi-506500), open form, space group i2, bound citrate
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas putida F1]]
[[Category: Al Obaidi NF]]
[[Category: Almo SC]]
[[Category: Bhosle R]]
[[Category: Chowdhury S]]
[[Category: Evans B]]
[[Category: Gerlt JA]]
[[Category: Hammonds J]]
[[Category: Hillerich B]]
[[Category: Imker HJ]]
[[Category: Love J]]
[[Category: Morisco LL]]
[[Category: Scott Glenn A]]
[[Category: Seidel RD]]
[[Category: Sojitra S]]
[[Category: Stead M]]
[[Category: Toro R]]
[[Category: Vetting MW]]
[[Category: Washington E]]
[[Category: Wasserman SR]]

Latest revision as of 18:39, 20 September 2023

Crystal structure of Pput_1285, a putative hydroxyproline epimerase from Pseudomonas putida f1 (target EFI-506500), open form, space group I2, bound citrateCrystal structure of Pput_1285, a putative hydroxyproline epimerase from Pseudomonas putida f1 (target EFI-506500), open form, space group I2, bound citrate

Structural highlights

4jbd is a 1 chain structure with sequence from Pseudomonas putida F1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

4HYPE_PSEP1 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 200-fold lower efficiency.[1]

See Also

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

4jbd, resolution 1.30Å

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