6ah8: Difference between revisions
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==Marine bacterial prolidase with promiscuous organophosphorus hydrolase activity== | |||
<StructureSection load='6ah8' size='340' side='right'caption='[[6ah8]], [[Resolution|resolution]] 2.61Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ah8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoalteromonas_lipolytica Pseudoalteromonas lipolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AH8 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]] 2.61Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6ah8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ah8 OCA], [https://pdbe.org/6ah8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ah8 RCSB], [https://www.ebi.ac.uk/pdbsum/6ah8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ah8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1I7CHQ2_9GAMM A0A1I7CHQ2_9GAMM] Splits dipeptides with a prolyl residue in the C-terminal position.[HAMAP-Rule:MF_01279][SAAS:SAAS01095084] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Enzyme promiscuity is critical to the acquisition of evolutionary plasticity in cells and can be recruited for high-value chemical synthesis or xenobiotic degradation. The molecular determinants of substrate ambiguity are essential to this activity; however, these details remain unknown. Here, we performed the directed evolution of a prolidase to enhance its initially weak paraoxonase activity. The in vitro evolution led to an unexpected 1,000,000-fold switch in substrate selectivity, with a 30-fold increase in paraoxon hydrolysis and 40,000-fold decrease in peptide hydrolysis. Structural and in silico analyses revealed enlarged catalytic cavities and substrate repositioning as responsible for rapid catalytic transitions between distinct chemical reactions. | |||
Repurposing a bacterial prolidase for organophosphorus hydrolysis: Reshaped catalytic cavity switches substrate selectivity.,Yang J, Xiao YZ, Li R, Liu Y, Long LJ Biotechnol Bioeng. 2020 Sep;117(9):2694-2702. doi: 10.1002/bit.27455. Epub 2020, Jun 26. PMID:32515491<ref>PMID:32515491</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ah8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudoalteromonas lipolytica]] | |||
[[Category: Jian Y]] | |||
Latest revision as of 12:30, 22 November 2023
Marine bacterial prolidase with promiscuous organophosphorus hydrolase activityMarine bacterial prolidase with promiscuous organophosphorus hydrolase activity
Structural highlights
FunctionA0A1I7CHQ2_9GAMM Splits dipeptides with a prolyl residue in the C-terminal position.[HAMAP-Rule:MF_01279][SAAS:SAAS01095084] Publication Abstract from PubMedEnzyme promiscuity is critical to the acquisition of evolutionary plasticity in cells and can be recruited for high-value chemical synthesis or xenobiotic degradation. The molecular determinants of substrate ambiguity are essential to this activity; however, these details remain unknown. Here, we performed the directed evolution of a prolidase to enhance its initially weak paraoxonase activity. The in vitro evolution led to an unexpected 1,000,000-fold switch in substrate selectivity, with a 30-fold increase in paraoxon hydrolysis and 40,000-fold decrease in peptide hydrolysis. Structural and in silico analyses revealed enlarged catalytic cavities and substrate repositioning as responsible for rapid catalytic transitions between distinct chemical reactions. Repurposing a bacterial prolidase for organophosphorus hydrolysis: Reshaped catalytic cavity switches substrate selectivity.,Yang J, Xiao YZ, Li R, Liu Y, Long LJ Biotechnol Bioeng. 2020 Sep;117(9):2694-2702. doi: 10.1002/bit.27455. Epub 2020, Jun 26. PMID:32515491[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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