8erj

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'''Unreleased structure'''
 
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The entry 8erj is ON HOLD until Paper Publication
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==Crystal structure of Fub7 in complex with E-2-aminocrotonate==
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<StructureSection load='8erj' size='340' side='right'caption='[[8erj]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
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Authors: Hai, Y.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8erj]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_fujikuroi Fusarium fujikuroi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ERJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ERJ FirstGlance]. <br>
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Description: Crystal structure of Fub7 in complex with E-2-aminocrotonate
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.16&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4LM:(2E)-2-{[(1E)-{3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYLIDENE]AMINO}BUT-2-ENOIC+ACID'>4LM</scene>, <scene name='pdbligand=WQF:(2S)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]but-3-enoic+acid'>WQF</scene></td></tr>
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[[Category: Hai, Y]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8erj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8erj OCA], [https://pdbe.org/8erj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8erj RCSB], [https://www.ebi.ac.uk/pdbsum/8erj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8erj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FUB7_GIBF5 FUB7_GIBF5] Sulfhydrylase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties (PubMed:26662839). L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (PubMed:26662839). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (PubMed:26662839). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (PubMed:26662839). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the O-acetylhomoserine FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (PubMed:26662839). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (PubMed:26662839).<ref>PMID:26662839</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Fusarium fujikuroi]]
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[[Category: Large Structures]]
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[[Category: Hai Y]]

Revision as of 07:04, 25 October 2023

Crystal structure of Fub7 in complex with E-2-aminocrotonate

PDB ID 8erj

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