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| | <StructureSection load='5dyq' size='340' side='right'caption='[[5dyq]], [[Resolution|resolution]] 1.66Å' scene=''> | | <StructureSection load='5dyq' size='340' side='right'caption='[[5dyq]], [[Resolution|resolution]] 1.66Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5dyq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Verma Verma]. 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 [http://proteopedia.org/fgij/fg.htm?mol=5DYQ FirstGlance]. <br> | + | <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='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></td></tr> | + | </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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VAB18032_16470, AbyU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=263358 VERMA])</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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5dyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dyq OCA], [http://pdbe.org/5dyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dyq RCSB], [http://www.ebi.ac.uk/pdbsum/5dyq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dyq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/F4F7G1_MICM1 F4F7G1_MICM1] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Verma]] | + | [[Category: Micromonospora maris AB-18-032]] |
| - | [[Category: Byrne, M J]] | + | [[Category: Byrne MJ]] |
| - | [[Category: Race, P R]] | + | [[Category: Race PR]] |
| - | [[Category: Abyssomicin]]
| + | |
| - | [[Category: Diels-alder]]
| + | |
| - | [[Category: Diels-alderase]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Polyketide]]
| + | |
| - | [[Category: Spirotetronate]]
| + | |
| - | [[Category: Tetronate]]
| + | |
| Structural highlights
Function
F4F7G1_MICM1
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Byrne MJ, Lees NR, Han LC, van der Kamp MW, Mulholland AJ, Stach JE, Willis CL, Race PR. The Catalytic Mechanism of a Natural Diels-Alderase Revealed in Molecular Detail. J Am Chem Soc. 2016 May 18;138(19):6095-8. doi: 10.1021/jacs.6b00232. Epub 2016, May 6. PMID:27140661 doi:http://dx.doi.org/10.1021/jacs.6b00232
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