1t0s

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{{Seed}}
 
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[[Image:1t0s.png|left|200px]]
 
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==Structure of the Toluene/o-Xylene Monooxygenase Hydroxylase with 4-bromophenol bound==
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The line below this paragraph, containing "STRUCTURE_1t0s", creates the "Structure Box" on the page.
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<StructureSection load='1t0s' size='340' side='right'caption='[[1t0s]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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>
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{{STRUCTURE_1t0s| PDB=1t0s | SCENE= }}
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O87799_STUST O87799_STUST]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t0/1t0s_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t0s ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Structure of the Toluene/o-Xylene Monooxygenase Hydroxylase with 4-bromophenol bound===
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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<ref>PMID:15096510</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1t0s" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15096510}}, adds the Publication Abstract to the page
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*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15096510 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15096510}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1T0S is a 3 chains structure of sequences from [http://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].
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==Reference==
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<ref group="xtra">PMID:15096510</ref><references group="xtra"/>
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[[Category: Pseudomonas stutzeri]]
[[Category: Pseudomonas stutzeri]]
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[[Category: Bard, J.]]
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[[Category: Bard J]]
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[[Category: Donato, A Di.]]
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[[Category: Di Donato A]]
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[[Category: Lippard, S J.]]
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[[Category: Lippard SJ]]
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[[Category: Sazinsky, M H.]]
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[[Category: Sazinsky MH]]
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[[Category: 4-bromophenol]]
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[[Category: 4-helix bundle]]
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[[Category: Carboxylate bridge]]
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[[Category: Channel]]
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[[Category: Diiron]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 11:04:50 2009''
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Current revision

Structure of the Toluene/o-Xylene Monooxygenase Hydroxylase with 4-bromophenol bound

PDB ID 1t0s

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