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| | ==Structure of the Toluene/o-Xylene Monooxygenase Hydroxylase with 4-bromophenol bound== | | ==Structure of the Toluene/o-Xylene Monooxygenase Hydroxylase with 4-bromophenol bound== |
| - | <StructureSection load='1t0s' size='340' side='right' caption='[[1t0s]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='1t0s' size='340' side='right'caption='[[1t0s]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1t0s]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_sewerinii"_bergey_et_al._1923 "achromobacter sewerinii" bergey et al. 1923]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T0S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1t0s]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T0S FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BML:4-BROMOPHENOL'>BML</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MCR:SULFANYLACETIC+ACID'>MCR</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</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]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">touA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316 "Achromobacter sewerinii" Bergey et al. 1923]), touE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316 "Achromobacter sewerinii" Bergey et al. 1923]), touB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316 "Achromobacter sewerinii" Bergey et al. 1923])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BML:4-BROMOPHENOL'>BML</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MCR:SULFANYLACETIC+ACID'>MCR</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene></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=1t0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0s OCA], [http://pdbe.org/1t0s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t0s RCSB], [http://www.ebi.ac.uk/pdbsum/1t0s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t0s ProSAT]</span></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=1t0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0s OCA], [https://pdbe.org/1t0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t0s RCSB], [https://www.ebi.ac.uk/pdbsum/1t0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t0s ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O87799_STUST O87799_STUST] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Monooxygenase|Monooxygenase]] | + | *[[Monooxygenase 3D structures|Monooxygenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Achromobacter sewerinii bergey et al. 1923]] | + | [[Category: Large Structures]] |
| - | [[Category: Bard, J]] | + | [[Category: Pseudomonas stutzeri]] |
| - | [[Category: Donato, A Di]] | + | [[Category: Bard J]] |
| - | [[Category: Lippard, S J]]
| + | [[Category: Di Donato A]] |
| - | [[Category: Sazinsky, M H]] | + | [[Category: Lippard SJ]] |
| - | [[Category: 4-bromophenol]] | + | [[Category: Sazinsky MH]] |
| - | [[Category: 4-helix bundle]] | + | |
| - | [[Category: Carboxylate bridge]]
| + | |
| - | [[Category: Channel]]
| + | |
| - | [[Category: Diiron]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
O87799_STUST
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The four-component toluene/o-xylene monooxygenase (ToMO) from Pseudomonas stutzeri OX1 is capable of oxidizing arenes, alkenes, and haloalkanes at a carboxylate-bridged diiron center similar to that of soluble methane monooxygenase (sMMO). The remarkable variety of substrates accommodated by ToMO invites applications ranging from bioremediation to the regio- and enantiospecific oxidation of hydrocarbons on an industrial scale. We report here the crystal structures of the ToMO hydroxylase (ToMOH), azido ToMOH, and ToMOH containing the product analogue 4-bromophenol to 2.3 A or greater resolution. The catalytic diiron(III) core resembles that of the sMMO hydroxylase, but aspects of the alpha2beta2gamma2 tertiary structure are notably different. Of particular interest is a 6-10 A-wide channel of approximately 35 A in length extending from the active site to the protein surface. The presence of three bromophenol molecules in this space confirms this route as a pathway for substrate entrance and product egress. An analysis of the ToMOH active site cavity offers insights into the different substrate specificities of multicomponent monooxygenases and explains the behavior of mutant forms of homologous enzymes described in the literature.
Crystal structure of the toluene/o-xylene monooxygenase hydroxylase from Pseudomonas stutzeri OX1. Insight into the substrate specificity, substrate channeling, and active site tuning of multicomponent monooxygenases.,Sazinsky MH, Bard J, Di Donato A, Lippard SJ J Biol Chem. 2004 Jul 16;279(29):30600-10. Epub 2004 Apr 19. PMID:15096510[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sazinsky MH, Bard J, Di Donato A, Lippard SJ. Crystal structure of the toluene/o-xylene monooxygenase hydroxylase from Pseudomonas stutzeri OX1. Insight into the substrate specificity, substrate channeling, and active site tuning of multicomponent monooxygenases. J Biol Chem. 2004 Jul 16;279(29):30600-10. Epub 2004 Apr 19. PMID:15096510 doi:10.1074/jbc.M400710200
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