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6ah7
From Proteopedia
(Difference between revisions)
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<StructureSection load='6ah7' size='340' side='right'caption='[[6ah7]], [[Resolution|resolution]] 2.38Å' scene=''> | <StructureSection load='6ah7' size='340' side='right'caption='[[6ah7]], [[Resolution|resolution]] 2.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6ah7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cgmcc_1.8499 Cgmcc 1.8499]. 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 [http:// | + | <table><tr><td colspan='2'>[[6ah7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cgmcc_1.8499 Cgmcc 1.8499]. 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 [http://proteopedia.org/fgij/fg.htm?mol=6AH7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pepQ, SAMN04487854_12236 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=570156 CGMCC 1.8499])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pepQ, SAMN04487854_12236 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=570156 CGMCC 1.8499])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xaa-Pro_dipeptidase Xaa-Pro dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.9 3.4.13.9] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xaa-Pro_dipeptidase Xaa-Pro dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.9 3.4.13.9] </span></td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ah7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ah7 OCA], [http://pdbe.org/6ah7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ah7 RCSB], [http://www.ebi.ac.uk/pdbsum/6ah7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ah7 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://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] | [[http://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> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6ah7" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 11:20, 23 September 2020
D45W/H226G mutant of marine bacterial prolidase
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