View source for 7pbg


==4-ethylphenol oxidase from Gulosibacter chungangensis: native structure==
<StructureSection load='7pbg' size='340' side='right'caption='[[7pbg]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PBG 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]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=7pbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pbg OCA], [https://pdbe.org/7pbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pbg RCSB], [https://www.ebi.ac.uk/pdbsum/7pbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pbg ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The vanillyl-alcohol oxidase (VAO) family is a rich source of biocatalysts for the oxidative bioconversion of phenolic compounds. Through genome mining and sequence comparisons, we found that several family members lack a generally conserved catalytic aspartate. This finding led us to study a VAO-homolog featuring a glutamate residue in place of the common aspartate. This 4-ethylphenol oxidase from Gulosibacter chungangensis (Gc4EO) shares 42% sequence identity with VAO, contains the same 8alpha-N3-histidyl-bound FAD and uses oxygen as electron acceptor. However, Gc4EO features a distinct substrate scope and product specificity as it is primarily effective in the dehydrogenation of para -substituted phenols with little generation of hydroxylated products. The three-dimensional structure shows that the characteristic glutamate side chain creates a closely packed environment that may limit water accessibility and thereby protect from hydroxylation. With its high thermal stability, well defined structural properties and high expression yields, Gc4EO may become a catalyst of choice for the specific dehydrogenation of phenolic compounds bearing small substituents.

Discovery, biocatalytic exploration and structural analysis of a 4-ethylphenol oxidase from Gulosibacter chungangensis.,Laura A, Gran-Scheuch A, Guo Y, Trajkovic M, Saifuddin M, Fraaije MW, Mattevi A Chembiochem. 2021 Sep 15. doi: 10.1002/cbic.202100457. PMID:34523783<ref>PMID:34523783</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Alvigini L]]
[[Category: Mattevi A]]