View source for 9gp0


==4-allyl syringol oxidase from Streptomyces cavernae: complex with Vanillyl alcohol==
<StructureSection load='9gp0' size='340' side='right'caption='[[9gp0]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9gp0]] 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=9GP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9GP0 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]] 1.75&#8491;</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=V55:4-HYDROXY-3-METHOXYBENZALDEHYDE'>V55</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=9gp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9gp0 OCA], [https://pdbe.org/9gp0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9gp0 RCSB], [https://www.ebi.ac.uk/pdbsum/9gp0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9gp0 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9gp0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces cavernae]]
[[Category: Alvigini L]]
[[Category: Mattevi A]]