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6ah7
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==D45W/H226G mutant of marine bacterial prolidase== | |
| + | <StructureSection load='6ah7' size='340' side='right'caption='[[6ah7]], [[Resolution|resolution]] 2.38Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ah7]] 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=6AH7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AH7 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]] 2.38Å</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=NA:SODIUM+ION'>NA</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=6ah7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ah7 OCA], [https://pdbe.org/6ah7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ah7 RCSB], [https://www.ebi.ac.uk/pdbsum/6ah7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ah7 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> |
| - | [[Category: Jian | + | <div class="pdbe-citations 6ah7" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudoalteromonas lipolytica]] | ||
| + | [[Category: Jian Y]] | ||
| + | [[Category: Lijuan L]] | ||
| + | [[Category: Yunzhu X]] | ||
Current revision
D45W/H226G mutant of marine bacterial prolidase
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