1t0r: Difference between revisions

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[[Image:1t0r.jpg|left|200px]]<br /><applet load="1t0r" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1t0r.jpg|left|200px]]
caption="1t0r, resolution 2.30&Aring;" />
 
'''Crystal Structure of the Toluene/o-xylene Monooxygenase Hydroxuylase from Pseudomonas stutzeri-azide bound'''<br />
{{Structure
|PDB= 1t0r |SIZE=350|CAPTION= <scene name='initialview01'>1t0r</scene>, resolution 2.30&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene> and <scene name='pdbligand=AZI:AZIDE ION'>AZI</scene>
|ACTIVITY=
|GENE= touA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316 Pseudomonas stutzeri]), touE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316 Pseudomonas stutzeri]), touB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316 Pseudomonas stutzeri])
}}
 
'''Crystal Structure of the Toluene/o-xylene Monooxygenase Hydroxuylase from Pseudomonas stutzeri-azide bound'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1T0R is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=OH:'>OH</scene> and <scene name='pdbligand=AZI:'>AZI</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0R OCA].  
1T0R is a [[Protein complex]] 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=1T0R OCA].  


==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15096510 15096510]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15096510 15096510]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Pseudomonas stutzeri]]
[[Category: Pseudomonas stutzeri]]
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[[Category: diiron]]
[[Category: diiron]]


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Revision as of 15:12, 20 March 2008

File:1t0r.jpg


PDB ID 1t0r

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands: , and
Gene: touA (Pseudomonas stutzeri), touE (Pseudomonas stutzeri), touB (Pseudomonas stutzeri)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the Toluene/o-xylene Monooxygenase Hydroxuylase from Pseudomonas stutzeri-azide bound


OverviewOverview

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.

About this StructureAbout this Structure

1T0R is a Protein complex structure of sequences from Pseudomonas stutzeri. Full crystallographic information is available from OCA.

ReferenceReference

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

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