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7nf4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of A. niger Fdc T395M R435P P438W variant (AnFdcII) in complex with prFMN== | |
| + | <StructureSection load='7nf4' size='340' side='right'caption='[[7nf4]], [[Resolution|resolution]] 1.69Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7nf4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger_CBS_513.88 Aspergillus niger CBS 513.88]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NF4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.69Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BYN:hydroxylated+prenyl-FMN'>BYN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=7nf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nf4 OCA], [https://pdbe.org/7nf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nf4 RCSB], [https://www.ebi.ac.uk/pdbsum/7nf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nf4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FDC1_ASPNC FDC1_ASPNC] Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of aroma metabolites.[HAMAP-Rule:MF_03196]<ref>PMID:26083754</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Isobutene is a high value gaseous alkene used as fuel additive and a chemical building block. As an alternative to fossil fuel derived isobutene, we here develop a modified mevalonate pathway for the production of isobutene from glucose in vivo. The final step in the pathway consists of the decarboxylation of 3-methylcrotonic acid, catalysed by an evolved ferulic acid decarboxylase (Fdc) enzyme. Fdc belongs to the prFMN-dependent UbiD enzyme family that catalyses reversible decarboxylation of (hetero)aromatic acids or acrylic acids with extended conjugation. Following a screen of an Fdc library for inherent 3-methylcrotonic acid decarboxylase activity, directed evolution yields variants with up to an 80-fold increase in activity. Crystal structures of the evolved variants reveal that changes in the substrate binding pocket are responsible for increased selectivity. Solution and computational studies suggest that isobutene cycloelimination is rate limiting and strictly dependent on presence of the 3-methyl group. | ||
| - | + | Directed evolution of prenylated FMN-dependent Fdc supports efficient in vivo isobutene production.,Saaret A, Villiers B, Stricher F, Anissimova M, Cadillon M, Spiess R, Hay S, Leys D Nat Commun. 2021 Sep 6;12(1):5300. doi: 10.1038/s41467-021-25598-0. PMID:34489427<ref>PMID:34489427</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7nf4" style="background-color:#fffaf0;"></div> |
| - | [[Category: Leys | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aspergillus niger CBS 513 88]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Leys D]] | ||
| + | [[Category: Saaret A]] | ||
Current revision
Structure of A. niger Fdc T395M R435P P438W variant (AnFdcII) in complex with prFMN
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