5ybs
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Fe(II)/(alpha)ketoglutarate-dependent dioxygenase PrhA-V150L/A232S in complex with berkeleyone A== | |
| + | <StructureSection load='5ybs' size='340' side='right' caption='[[5ybs]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ybs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YBS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YBS FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8TC:berkeleyone+A'>8TC</scene>, <scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=5ybs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ybs OCA], [http://pdbe.org/5ybs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ybs RCSB], [http://www.ebi.ac.uk/pdbsum/5ybs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ybs ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Non-heme iron and alpha-ketoglutarate (alphaKG) oxygenases catalyze remarkably diverse reactions using a single ferrous ion cofactor. A major challenge in studying this versatile family of enzymes is to understand their structure-function relationship. AusE from Aspergillus nidulans and PrhA from Penicillium brasilianum are two highly homologous Fe(II)/alphaKG oxygenases in fungal meroterpenoid biosynthetic pathways that use preaustinoid A1 as a common substrate to catalyze divergent rearrangement reactions to form the spiro-lactone in austinol and cycloheptadiene moiety in paraherquonin, respectively. Herein, we report the comparative structural study of AusE and PrhA, which led to the identification of three key active site residues that control their reactivity. Structure-guided mutagenesis of these residues results in successful interconversion of AusE and PrhA functions as well as generation of the PrhA double and triple mutants with expanded catalytic repertoire. Manipulation of the multifunctional Fe(II)/alphaKG oxygenases thus provides an excellent platform for the future development of biocatalysts. | ||
| - | + | Structure function and engineering of multifunctional non-heme iron dependent oxygenases in fungal meroterpenoid biosynthesis.,Nakashima Y, Mori T, Nakamura H, Awakawa T, Hoshino S, Senda M, Senda T, Abe I Nat Commun. 2018 Jan 9;9(1):104. doi: 10.1038/s41467-017-02371-w. PMID:29317628<ref>PMID:29317628</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5ybs" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Nakashima, Y]] | ||
| + | [[Category: Senda, M]] | ||
| + | [[Category: Alpha-kegoglutarate-dependent dioxygenase]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 18:28, 24 January 2018
Fe(II)/(alpha)ketoglutarate-dependent dioxygenase PrhA-V150L/A232S in complex with berkeleyone A
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