View source for 5dyq


==AbyU L73M L139M==
<StructureSection load='5dyq' size='340' side='right'caption='[[5dyq]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5dyq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonospora_maris_AB-18-032 Micromonospora maris AB-18-032]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DYQ 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]] 1.66&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5dyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dyq OCA], [https://pdbe.org/5dyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dyq RCSB], [https://www.ebi.ac.uk/pdbsum/5dyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dyq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F4F7G1_MICM1 F4F7G1_MICM1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Diels-Alder reaction, a [4 + 2] cycloaddition of a conjugated diene to a dienophile, is one of the most powerful reactions in synthetic chemistry. Biocatalysts capable of unlocking new and efficient Diels-Alder reactions would have major impact. Here we present a molecular-level description of the reaction mechanism of the spirotetronate cyclase AbyU, an enzyme shown here to be a bona fide natural Diels-Alderase. Using enzyme assays, X-ray crystal structures, and simulations of the reaction in the enzyme, we reveal how linear substrate chains are contorted within the AbyU active site to facilitate a transannular pericyclic reaction. This study provides compelling evidence for the existence of a natural enzyme evolved to catalyze a Diels-Alder reaction and shows how catalysis is achieved.

The Catalytic Mechanism of a Natural Diels-Alderase Revealed in Molecular Detail.,Byrne MJ, Lees NR, Han LC, van der Kamp MW, Mulholland AJ, Stach JE, Willis CL, Race PR J Am Chem Soc. 2016 May 18;138(19):6095-8. doi: 10.1021/jacs.6b00232. Epub 2016, May 6. PMID:27140661<ref>PMID:27140661</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5dyq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Micromonospora maris AB-18-032]]
[[Category: Byrne MJ]]
[[Category: Race PR]]