9gov

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'''Unreleased structure'''
 
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The entry 9gov is ON HOLD
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==4-Allyl syringol oxidase from Streptomyces cavernae: complex with Propanol syringol==
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<StructureSection load='9gov' size='340' side='right'caption='[[9gov]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9gov]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_cavernae Streptomyces cavernae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9GOV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9GOV FirstGlance]. <br>
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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&#8491;</td></tr>
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<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=QBF:2,6-dimethoxy-4-(3-oxidanylpropyl)phenol'>QBF</scene></td></tr>
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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=9gov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9gov OCA], [https://pdbe.org/9gov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9gov RCSB], [https://www.ebi.ac.uk/pdbsum/9gov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9gov ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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4-Phenol oxidases are proposed to be involved in the utilization of lignin-derived aromatic compounds. While enzymes with selectivity towards 4-hydroxyphenyl and guaiacyl motifs are well described, we identified the first syringyl-specific oxidase from Streptomyces cavernae (Sc4ASO) only very recently. Here, in-depth studies were conducted to unravel the molecular origins of the outstanding selectivity of Sc4ASO. Kinetic experiments revealed high activities on dimethoxylated substrates (up to 2.9 +/- 0.1 s(-1)), but also strong cooperativity between both protein subunits, as well as substrate inhibition in dependency of ortho methoxylation and chain length of the para substituent. Rapid mixing kinetics in combination with the determination of the crystal structure in complex with three substrates allowed to connect the kinetic behavior with never-observed positioning of the conserved residue Y471. Ultimately, the catalytic potential of Sc4ASO was investigated in a 100 mL scale cascade reaction to produce the natural product syringaresinol.
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Authors: Alvigini, L., Mattevi, A.
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Kinetic and structural investigation of the 4-allyl syringol oxidase from Streptomyces cavernae.,Eggerichs D, Weddeling HG, Alvigini L, Rapsch T, Weindorf N, Mattevi A, Tischler D Arch Biochem Biophys. 2025 Jan 25;765:110320. doi: 10.1016/j.abb.2025.110320. PMID:39870290<ref>PMID:39870290</ref>
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Description: 4-Allyl syringol oxidase from Streptomyces cavernae: complex with Propanol syringol
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Alvigini, L]]
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<div class="pdbe-citations 9gov" style="background-color:#fffaf0;"></div>
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[[Category: Mattevi, A]]
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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: Large Structures]]
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[[Category: Streptomyces cavernae]]
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[[Category: Alvigini L]]
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[[Category: Mattevi A]]

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4-Allyl syringol oxidase from Streptomyces cavernae: complex with Propanol syringol

PDB ID 9gov

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