This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
5dyq
From Proteopedia
(Difference between revisions)
m (Protected "5dyq" [edit=sysop:move=sysop]) |
|||
| (3 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==AbyU L73M L139M== | |
| + | <StructureSection load='5dyq' size='340' side='right'caption='[[5dyq]], [[Resolution|resolution]] 1.66Å' 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]] 1.66Å</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5dyq" style="background-color:#fffaf0;"></div> |
| - | [[Category: Byrne | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Micromonospora maris AB-18-032]] | ||
| + | [[Category: Byrne MJ]] | ||
| + | [[Category: Race PR]] | ||
Current revision
AbyU L73M L139M
| |||||||||||
