5ybp: Difference between revisions
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==Fe(II)/(alpha)ketoglutarate-dependent dioxygenase PrhA-V150L/A232S in complex with preaustinoid A1== | |||
<StructureSection load='5ybp' size='340' side='right' caption='[[5ybp]], [[Resolution|resolution]] 2.31Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ybp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YBP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YBP FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8SX:preaustinoid+A1'>8SX</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=5ybp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ybp OCA], [http://pdbe.org/5ybp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ybp RCSB], [http://www.ebi.ac.uk/pdbsum/5ybp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ybp 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 5ybp" 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 21:28, 24 January 2018
Fe(II)/(alpha)ketoglutarate-dependent dioxygenase PrhA-V150L/A232S in complex with preaustinoid A1Fe(II)/(alpha)ketoglutarate-dependent dioxygenase PrhA-V150L/A232S in complex with preaustinoid A1
Structural highlights
Publication Abstract from PubMedNon-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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