6ghw: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "6ghw" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
==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]] | |||
