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| | <StructureSection load='7cp7' size='340' side='right'caption='[[7cp7]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='7cp7' size='340' side='right'caption='[[7cp7]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7cp7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_fumigatus_z5 Aspergillus fumigatus z5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CP7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7CP7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7cp7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus_Z5 Aspergillus fumigatus Z5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CP7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Y699_04337 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1437362 Aspergillus fumigatus Z5])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7cp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cp7 OCA], [http://pdbe.org/7cp7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7cp7 RCSB], [http://www.ebi.ac.uk/pdbsum/7cp7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7cp7 ProSAT]</span></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=7cp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cp7 OCA], [https://pdbe.org/7cp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cp7 RCSB], [https://www.ebi.ac.uk/pdbsum/7cp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cp7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0J5T0B0_ASPFM A0A0J5T0B0_ASPFM] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspergillus fumigatus z5]] | + | [[Category: Aspergillus fumigatus Z5]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hara, K]] | + | [[Category: Hara K]] |
| - | [[Category: Hashimoto, H]] | + | [[Category: Hashimoto H]] |
| - | [[Category: Kishimoto, S]] | + | [[Category: Kishimoto S]] |
| - | [[Category: Matsushita, T]] | + | [[Category: Matsushita T]] |
| - | [[Category: Watanabe, K]] | + | [[Category: Watanabe K]] |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
A0A0J5T0B0_ASPFM
Publication Abstract from PubMed
Biosynthesis of fungal nonribosomal peptides frequently involves redox enzymes such as flavin-containing monooxygenase (FMO) to introduce complexity into the core chemical structure. One such example is the formation of spiro-carbons catalyzed by various oxidases. Because many chemically complex spiro-carbon-bearing natural products exhibit useful biological activities, understanding the mechanism of spiro-carbon biosynthesis is of great interest. We previously identified FqzB, an FMO from the fumiquinazoline biosynthetic pathway responsible for epoxidation of fumiquinazoline F that crosstalks with the fumitremorgin biosynthetic pathway to form spirotryprostatin A via epoxidation of the precursor fumitremorgin C. What makes FqzB more interesting is its relaxed substrate specificity, where it can accept a range of other substrates, including tryprostatins A and B along with its original substrate fumiquinazoline F. Here, we characterized FqzB crystallographically and examined FqzB and its site-specific mutants kinetically to understand how this promiscuous epoxidase works. Furthermore, the mutagenesis studies as well as computational docking experiments between the FqzB crystal structure and its known substrates spirotryprostatin A and B, as well as fumitremorgin C and fumiquinazoline F, provided insight into potential modes of substrate recognition and the source of broad substrate tolerance exhibited by this epoxidase. This study serves as a foundation for further characterization and engineering of this redox enzyme, which has potential utility as a valuable catalyst with broad substrate tolerance and an ability to introduce chemical complexity into carbon frameworks for chemoenzymatic and biosynthetic applications.
Structural and Functional Analyses of a Spiro-Carbon-Forming, Highly Promiscuous Epoxidase from Fungal Natural Product Biosynthesis.,Matsushita T, Kishimoto S, Hara K, Hashimoto H, Watanabe K Biochemistry. 2020 Dec 17. doi: 10.1021/acs.biochem.0c00896. PMID:33332106[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Matsushita T, Kishimoto S, Hara K, Hashimoto H, Watanabe K. Structural and Functional Analyses of a Spiro-Carbon-Forming, Highly Promiscuous Epoxidase from Fungal Natural Product Biosynthesis. Biochemistry. 2020 Dec 17. doi: 10.1021/acs.biochem.0c00896. PMID:33332106 doi:http://dx.doi.org/10.1021/acs.biochem.0c00896
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