7eeh
From Proteopedia
(Difference between revisions)
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==Selenomethionine labeled Fe(II)/(alpha)ketoglutarate-dependent dioxygenase TqaL== | ==Selenomethionine labeled Fe(II)/(alpha)ketoglutarate-dependent dioxygenase TqaL== | ||
| - | <StructureSection load='7eeh' size='340' side='right'caption='[[7eeh]]' scene=''> | + | <StructureSection load='7eeh' size='340' side='right'caption='[[7eeh]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EEH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7eeh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chrysonilia_crassa Chrysonilia crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EEH FirstGlance]. <br> |
| - | </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=7eeh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eeh OCA], [https://pdbe.org/7eeh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eeh RCSB], [https://www.ebi.ac.uk/pdbsum/7eeh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eeh ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B14A6.180 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5141 Chrysonilia crassa])</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=7eeh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eeh OCA], [https://pdbe.org/7eeh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eeh RCSB], [https://www.ebi.ac.uk/pdbsum/7eeh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eeh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Aziridine is a characteristically reactive molecule with increased bioactivity due to its strained ring structure. Here, we investigated the biosynthesis of 2-aminoisobutyric acid (AIB) in Penicillium , and successfully reconstituted the three-step biosynthesis from L-Val to AIB in vitro . This previously unknown aziridine formation pathway proceeded with the non-heme iron and a -ketoglutarate-dependent (Fe(II)/ alpha KG) oxygenase TqaL, followed by aziridine ring opening by the haloalkanoic acid dehalogenase (HAD)-type hydrolase TqaF, and subsequent oxidative decarboxylation by the NovR/CloR-like non-heme iron oxygenase TqaM. Furthermore, the X-ray crystal structure of the C-N bond forming Fe(II)/ alpha KG oxygenase TqaL was solved at 2.0 A resolution. This work presents the first molecular basis for aziridine biogenesis, thereby expanding the catalytic repertoire of the Fe(II)/ alpha KG oxygenases. We also report the unique aziridine ring opening by a HAD-type hydrolase and the remarkable oxidative decarboxylation by a non-heme iron oxygenase to produce AIB. | ||
| + | |||
| + | Aziridine formation by a Fe(II)/alpha-ketoglutarate dependent oxygenase and 2-aminoisobutyrate biosynthesis in fungi.,Abe I, Bunno R, Awakawa T, Mori T Angew Chem Int Ed Engl. 2021 May 11. doi: 10.1002/anie.202104644. PMID:33973699<ref>PMID:33973699</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7eeh" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Chrysonilia crassa]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Abe I]] | + | [[Category: Abe, I]] |
| - | [[Category: Awakawa T]] | + | [[Category: Awakawa, T]] |
| - | [[Category: Bunno R]] | + | [[Category: Bunno, R]] |
| - | [[Category: Mori T]] | + | [[Category: Mori, T]] |
| + | [[Category: Alpha-ketoglutarate dependent dioxygenase]] | ||
| + | [[Category: Aziridine]] | ||
| + | [[Category: Biosynthesis]] | ||
| + | [[Category: Oxidoreductase]] | ||
Current revision
Selenomethionine labeled Fe(II)/(alpha)ketoglutarate-dependent dioxygenase TqaL
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