5fhi
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5fhi is ON HOLD Authors: HARA, K., HASHIMOTO, H., YAMAMOTO, T., TSUNEMATSU, Y., WATANABE, K. Description: Category: Unreleased Structures [[Ca...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystallographic structure of PsoE without Co== | |
| - | + | <StructureSection load='5fhi' size='340' side='right'caption='[[5fhi]], [[Resolution|resolution]] 2.41Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5fhi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus_Af293 Aspergillus fumigatus Af293]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FHI 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]] 2.41Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fhi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fhi OCA], [https://pdbe.org/5fhi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fhi RCSB], [https://www.ebi.ac.uk/pdbsum/5fhi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fhi ProSAT]</span></td></tr> |
| - | [[Category: Hashimoto | + | </table> |
| - | [[Category: | + | == Function == |
| - | [[Category: | + | [https://www.uniprot.org/uniprot/PSOE_ASPFU PSOE_ASPFU] Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of pseurotin A, a competitive inhibitor of chitin synthase and an inducer of nerve-cell proliferation (PubMed:24082142, PubMed:24939566). The PKS-NRPS hybrid synthetase psoA is responsible for the biosynthesis of azaspirene, one of the first intermediates having the 1-oxa-7-azaspiro[4,4]-non-2-ene-4,6-dione core of pseurotin, via condensation of one acetyl-CoA, 4 malonyl-CoA, and a L-phenylalanine molecule (PubMed:24082142, PubMed:24939566). The dual-functional monooxygenase/methyltransferase psoF seems to be involved in the addition of the C3 methyl group onto the pseurotin scaffold (PubMed:24939566). Azaspirene is then converted to synerazol through 4 steps including oxidation of C17 by the cytochrome P450 monooxygenase psoD, O-methylation of the hydroxy group of C8 by the methyltransferase psoC, and the trans-to-cis isomerization of the C13 olefin by the glutathione S-transferase psoE (PubMed:24939566, PubMed:27072782). The fourth step of synerazol production is performed by the dual-functional monooxygenase/methyltransferase psoF which seems to catalyze the epoxidation of the intermediate deepoxy-synerazol (PubMed:24939566). Synerazol can be attacked by a water molecule nonenzymatically at two different positions to yield two diol products, pseurotin A and pseurotin D (PubMed:24939566).<ref>PMID:24082142</ref> <ref>PMID:24939566</ref> <ref>PMID:27072782</ref> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aspergillus fumigatus Af293]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hara K]] | ||
| + | [[Category: Hashimoto H]] | ||
| + | [[Category: Tsunematsu Y]] | ||
| + | [[Category: Watanabe K]] | ||
| + | [[Category: Yamamoto T]] | ||
Current revision
Crystallographic structure of PsoE without Co
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