5tdv

From Proteopedia

(Difference between revisions)

Revision as of 04:55, 12 April 2017

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

Structural highlights

5tdv is a 8 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	5tds, 5tdt, 5tdu
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3] [TMOA_PSEME] Hydroxylase subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol.^[4] ^[5] [TMOB_PSEME] Subunit T4moB of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol.^[6] ^[7] [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^[8]

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

References

↑ Hemmi H, Studts JM, Chae YK, Song J, Markley JL, Fox BG. Solution structure of the toluene 4-monooxygenase effector protein (T4moD). Biochemistry. 2001 Mar 27;40(12):3512-24. PMID:11297417
↑ Lountos GT, Mitchell KH, Studts JM, Fox BG, Orville AM. Crystal structures and functional studies of T4moD, the toluene 4-monooxygenase catalytic effector protein. Biochemistry. 2005 May 17;44(19):7131-42. PMID:15882052 doi:10.1021/bi047459g
↑ Bailey LJ, McCoy JG, Phillips GN Jr, Fox BG. Structural consequences of effector protein complex formation in a diiron hydroxylase. Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19194-8. Epub 2008 Nov 25. PMID:19033467
↑ Elsen NL, Bailey LJ, Hauser AD, Fox BG. Role for threonine 201 in the catalytic cycle of the soluble diiron hydroxylase toluene 4-monooxygenase. Biochemistry. 2009 May 12;48(18):3838-46. PMID:19290655 doi:10.1021/bi900144a
↑ Bailey LJ, Fox BG. Crystallographic and catalytic studies of the peroxide-shunt reaction in a diiron hydroxylase. Biochemistry. 2009 Sep 29;48(38):8932-9. PMID:19705873 doi:10.1021/bi901150a
↑ Elsen NL, Bailey LJ, Hauser AD, Fox BG. Role for threonine 201 in the catalytic cycle of the soluble diiron hydroxylase toluene 4-monooxygenase. Biochemistry. 2009 May 12;48(18):3838-46. PMID:19290655 doi:10.1021/bi900144a
↑ Bailey LJ, Fox BG. Crystallographic and catalytic studies of the peroxide-shunt reaction in a diiron hydroxylase. Biochemistry. 2009 Sep 29;48(38):8932-9. PMID:19705873 doi:10.1021/bi901150a
↑ 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 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5tdv is ON HOLD  until Paper Publication
+==Intermediate O2 diiron complex in the Q228A variant of Toluene 4-moonoxygenase (T4moHD)==
+<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. 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>
+</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>
+<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='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.
+<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.
-Authors: Bailey, L.J., Acheson, J.F., Fox, B.G.
+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>
-Description: Intermediate O2 diiron complex in the Q228A variant of Toluene 4-moonoxygenase (T4moHD)
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Fox, B.G]]
+<div class="pdbe-citations 5tdv" style="background-color:#fffaf0;"></div>
-[[Category: Bailey, L.J]]
+== References ==
-[[Category: Acheson, J.F]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Acheson, J F]]
+[[Category: Bailey, L J]]
+[[Category: Fox, B G]]
+[[Category: Complex]]
+[[Category: Diiron]]
+[[Category: Oxidoreductase]]
+[[Category: Oxygen activation]]

5tdv

From Proteopedia

Revision as of 04:55, 12 April 2017

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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