5dap: Difference between revisions
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==Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AsqJ== | ==Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AsqJ== | ||
<StructureSection load='5dap' size='340' side='right' caption='[[5dap]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='5dap' size='340' side='right'caption='[[5dap]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5dap]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DAP OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5dap]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_nidulans Aspergillus nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DAP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5DAP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4nao|4nao]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4nao|4nao]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AN9227.2, ANIA_09227 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=227321 Aspergillus nidulans])</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=5dap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dap OCA], [http://pdbe.org/5dap PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dap RCSB], [http://www.ebi.ac.uk/pdbsum/5dap PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dap ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aspergillus nidulans]] | |||
[[Category: Large Structures]] | |||
[[Category: Braeuer, A]] | [[Category: Braeuer, A]] | ||
[[Category: Groll, M]] | [[Category: Groll, M]] |
Revision as of 10:57, 8 April 2020
Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AsqJFe(II)/(alpha)ketoglutarate-dependent dioxygenase AsqJ
Structural highlights
Publication Abstract from PubMedMultienzymatic cascades are responsible for the biosynthesis of natural products and represent a source of inspiration for synthetic chemists. The FeII /alpha-ketoglutarate-dependent dioxygenase AsqJ from Aspergillus nidulans is outstanding because it stereoselectively catalyzes both a ferryl-induced desaturation reaction and epoxidation on a benzodiazepinedione. Interestingly, the enzymatically formed spiro epoxide spring-loads the 6,7-bicyclic skeleton for non-enzymatic rearrangement into the 6,6-bicyclic scaffold of the quinolone alkaloid 4'-methoxyviridicatin. Herein, we report different crystal structures of the protein in the absence and presence of synthesized substrates, surrogates, and intermediates that mimic the various stages of the reaction cycle of this exceptional dioxygenase. Structure of the Dioxygenase AsqJ: Mechanistic Insights into a One-Pot Multistep Quinolone Antibiotic Biosynthesis.,Brauer A, Beck P, Hintermann L, Groll M Angew Chem Int Ed Engl. 2015 Nov 10. doi: 10.1002/anie.201507835. PMID:26553478[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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