View source for 5tds


==Toluene bound in the resting active site of toluene 4-monooxygenase (T4moH)==
<StructureSection load='5tds' size='340' side='right'caption='[[5tds]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5tds]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_mendocina Pseudomonas mendocina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TDS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TDS 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]] 1.719&#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=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MBN:TOLUENE'>MBN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5tds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tds OCA], [https://pdbe.org/5tds PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tds RCSB], [https://www.ebi.ac.uk/pdbsum/5tds PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tds ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TMOA_PSEME TMOA_PSEME] Hydroxylase subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol.<ref>PMID:19290655</ref> <ref>PMID:19705873</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Electrophilic aromatic substitution is one of the most important and recognizable classes of organic chemical transformation. Enzymes create the strong electrophiles that are needed for these highly energetic reactions by using O2, electrons, and metals or other cofactors. Although the nature of the oxidants that carry out electrophilic aromatic substitution has been deduced from many approaches, it has been difficult to determine their structures. Here we show the structure of a diiron hydroxylase intermediate formed during a reaction with toluene. Density functional theory geometry optimizations of an active site model reveal that the intermediate is an arylperoxo Fe2+/Fe3+ species with delocalized aryl radical character. The structure suggests that a carboxylate ligand of the diiron centre may trigger homolytic cleavage of the O-O bond by transferring a proton from a metal-bound water. Our work provides the spatial and electronic constraints needed to propose a comprehensive mechanism for diiron enzyme arene hydroxylation that accounts for many prior experimental results.

In-crystal reaction cycle of a toluene-bound diiron hydroxylase.,Acheson JF, Bailey LJ, Brunold TC, Fox BG Nature. 2017 Mar 27. doi: 10.1038/nature21681. PMID:28346937<ref>PMID:28346937</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5tds" style="background-color:#fffaf0;"></div>

==See Also==
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas mendocina]]
[[Category: Acheson JF]]
[[Category: Fox BG]]