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5tdv

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Intermediate O2 diiron complex in the Q228A variant of Toluene 4-moonoxygenase (T4moHD)

Structural highlights

5tdv is a 8 chain structure with sequence from Pseudomonas mendocina. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.001Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TMOE_PSEME Subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5tdv"

Categories: Large Structures | Pseudomonas mendocina | Acheson JF | Bailey LJ | Fox BG

@@ Line 3: / Line 3: @@
 <StructureSection load='5tdv' size='340' side='right'caption='[[5tdv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5tdv]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25411 Atcc 25411]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TDV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TDV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5tdv]] is a 8 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=5TDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TDV FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PER:PEROXIDE+ION'>PER</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.001&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tds|5tds]], [[5tdt|5tdt]], [[5tdu|5tdu]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PER:PEROXIDE+ION'>PER</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tmoA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 ATCC 25411]), tmoE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 ATCC 25411]), tmoB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 ATCC 25411]), tmoD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 ATCC 25411])</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=5tdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdv OCA], [https://pdbe.org/5tdv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tdv RCSB], [https://www.ebi.ac.uk/pdbsum/5tdv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdv ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdv OCA], [http://pdbe.org/5tdv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tdv RCSB], [http://www.ebi.ac.uk/pdbsum/5tdv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdv ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TMOD_PSEME TMOD_PSEME]] Effector protein subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol. Required for optimal efficiency and specificity of the holoenzyme.<ref>PMID:11297417</ref> <ref>PMID:15882052</ref> <ref>PMID:19033467</ref>  [[http://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>  [[http://www.uniprot.org/uniprot/TMOB_PSEME TMOB_PSEME]] Subunit T4moB of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol.<ref>PMID:19290655</ref> <ref>PMID:19705873</ref>  [[http://www.uniprot.org/uniprot/TMOE_PSEME TMOE_PSEME]] Subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol.
+[https://www.uniprot.org/uniprot/TMOE_PSEME TMOE_PSEME] Subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 25411]]
 [[Category: Large Structures]]
-[[Category: Acheson, J F]]
+[[Category: Pseudomonas mendocina]]
-[[Category: Bailey, L J]]
+[[Category: Acheson JF]]
-[[Category: Fox, B G]]
+[[Category: Bailey LJ]]
-[[Category: Complex]]
+[[Category: Fox BG]]
-[[Category: Diiron]]
-[[Category: Oxidoreductase]]
-[[Category: Oxygen activation]]

5tdv

From Proteopedia

Current revision

Intermediate O2 diiron complex in the Q228A variant of Toluene 4-moonoxygenase (T4moHD)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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