6ghw
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Substituting the prolines of 4-oxalocrotonate tautomerase with non-canonical analogue (2S)-3,4-dehydroproline== | |
| + | <StructureSection load='6ghw' size='340' side='right' caption='[[6ghw]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ghw]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GHW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GHW FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=8LJ:'>8LJ</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-hydroxymuconate_tautomerase 2-hydroxymuconate tautomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.2.6 5.3.2.6] </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=6ghw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ghw OCA], [http://pdbe.org/6ghw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ghw RCSB], [http://www.ebi.ac.uk/pdbsum/6ghw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ghw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/4OT1_PSEPU 4OT1_PSEPU]] Catalyzes the ketonization of 2-hydroxymuconate stereoselectively to yield 2-oxo-3-hexenedioate.<ref>PMID:1339435</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The enzyme 4-oxalocrotonate tautomerase shows remarkable catalytic versatility due to the secondary amine of its N-terminal proline moiety. In this work, we incorporated a range of proline analogues into the enzyme and examined the effects on structure and activity. While the structure of the enzyme remained unperturbed, its promiscuous Michael-type activity was severely affected. This finding demonstrates how atomic changes in a biocatalytic system can abolish its activity. Our work provides a toolbox for successful generation of enzyme variants with non-canonical catalytic proline analogues. | ||
| - | + | Substituting the catalytic proline of 4-oxalocrotonate tautomerase with non-canonical analogues reveals a finely tuned catalytic system.,Lukesch MS, Pavkov-Keller T, Gruber K, Zangger K, Wiltschi B Sci Rep. 2019 Feb 25;9(1):2697. doi: 10.1038/s41598-019-39484-9. PMID:30804446<ref>PMID:30804446</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6ghw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: 2-hydroxymuconate tautomerase]] | ||
| + | [[Category: Gruber, K]] | ||
| + | [[Category: Lukesch, M S]] | ||
| + | [[Category: Pavkov-Keller, T]] | ||
| + | [[Category: Wiltschi, B]] | ||
| + | [[Category: 4-dehydroproline]] | ||
| + | [[Category: Isomerase]] | ||
| + | [[Category: Non-canonical amino acid]] | ||
Revision as of 07:28, 6 March 2019
Substituting the prolines of 4-oxalocrotonate tautomerase with non-canonical analogue (2S)-3,4-dehydroproline
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