5dav
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AsqJ in complex with 4-Methoxydehydrocyclopeptin== |
| + | <StructureSection load='5dav' size='340' side='right' caption='[[5dav]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5dav]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DAV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DAV FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=58J:4-METHOXYDEHYDROCYCLOPEPTIN'>58J</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dap|5dap]]</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=5dav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dav OCA], [http://pdbe.org/5dav PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dav RCSB], [http://www.ebi.ac.uk/pdbsum/5dav PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Multienzymatic 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<ref>PMID:26553478</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5dav" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Braeuer, A]] | ||
[[Category: Groll, M]] | [[Category: Groll, M]] | ||
| - | [[Category: | + | [[Category: 4-methoxydehydrocyclopeptin]] |
| + | [[Category: Alkaloid]] | ||
| + | [[Category: Antibiotic]] | ||
| + | [[Category: Biosynthesis]] | ||
| + | [[Category: Desaturase]] | ||
| + | [[Category: Epoxidase]] | ||
| + | [[Category: Fragmentation]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Viridicatin]] | ||
Revision as of 04:36, 1 December 2015
Fe(II)/(alpha)ketoglutarate-dependent dioxygenase AsqJ in complex with 4-Methoxydehydrocyclopeptin
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