1o7n: Difference between revisions

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New page: left|200px<br /> <applet load="1o7n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o7n, resolution 1.40Å" /> '''NAPHTHALENE 1,2-DIO...
 
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[[Image:1o7n.gif|left|200px]]<br />
<applet load="1o7n" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1o7n, resolution 1.40&Aring;" />
'''NAPHTHALENE 1,2-DIOXYGENASE, TERNARY COMPLEX WITH DIOXYGEN AND INDOLE'''<br />


==Overview==
==NAPHTHALENE 1,2-DIOXYGENASE, TERNARY COMPLEX WITH DIOXYGEN AND INDOLE==
Binding of oxygen to iron is exploited in several biological and chemical, processes. Although computational and spectroscopic results have suggested, side-on binding, only end-on binding of oxygen to iron has been observed, in crystal structures. We have determined structures of naphthalene, dioxygenase that show a molecular oxygen species bound to the mononuclear, iron in a side-on fashion. In a complex with substrate and dioxygen, the, dioxygen molecule is lined up for an attack on the double bond of the, aromatic substrate. The structures reported here provide the basis for a, reaction mechanism and for the high stereospecificity of the reaction, catalyzed by naphthalene dioxygenase.
<StructureSection load='1o7n' size='340' side='right'caption='[[1o7n]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1o7n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O7N FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=IND:INDOLE'>IND</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1o7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7n OCA], [https://pdbe.org/1o7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o7n RCSB], [https://www.ebi.ac.uk/pdbsum/1o7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7n ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NDOB_PSEPU NDOB_PSEPU] Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-naphthalene dihydrodiol.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/1o7n_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1o7n ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Binding of oxygen to iron is exploited in several biological and chemical processes. Although computational and spectroscopic results have suggested side-on binding, only end-on binding of oxygen to iron has been observed in crystal structures. We have determined structures of naphthalene dioxygenase that show a molecular oxygen species bound to the mononuclear iron in a side-on fashion. In a complex with substrate and dioxygen, the dioxygen molecule is lined up for an attack on the double bond of the aromatic substrate. The structures reported here provide the basis for a reaction mechanism and for the high stereospecificity of the reaction catalyzed by naphthalene dioxygenase.


==About this Structure==
Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron.,Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S Science. 2003 Feb 14;299(5609):1039-42. PMID:12586937<ref>PMID:12586937</ref>
1O7N is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]] with SO4, FE, EDO, IND, OXY and FES as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.12.12 1.14.12.12]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O7N OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron., Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S, Science. 2003 Feb 14;299(5609):1039-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12586937 12586937]
</div>
[[Category: Protein complex]]
<div class="pdbe-citations 1o7n" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Eklund, H.]]
[[Category: Eklund H]]
[[Category: Gibson, D.T.]]
[[Category: Gibson DT]]
[[Category: Karlsson, A.]]
[[Category: Karlsson A]]
[[Category: Parales, J.V.]]
[[Category: Parales JV]]
[[Category: Parales, R.E.]]
[[Category: Parales RE]]
[[Category: Ramaswamy, S.]]
[[Category: Ramaswamy S]]
[[Category: EDO]]
[[Category: FE]]
[[Category: FES]]
[[Category: IND]]
[[Category: OXY]]
[[Category: SO4]]
[[Category: aromatic hydrocarbon catabolism]]
[[Category: enzyme-substrate complex]]
[[Category: iron-sulfur]]
[[Category: non-heme iron dioxygenase]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:30:43 2007''

Latest revision as of 15:29, 13 December 2023

NAPHTHALENE 1,2-DIOXYGENASE, TERNARY COMPLEX WITH DIOXYGEN AND INDOLENAPHTHALENE 1,2-DIOXYGENASE, TERNARY COMPLEX WITH DIOXYGEN AND INDOLE

Structural highlights

1o7n is a 2 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.4Å
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NDOB_PSEPU Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-naphthalene dihydrodiol.

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

Binding of oxygen to iron is exploited in several biological and chemical processes. Although computational and spectroscopic results have suggested side-on binding, only end-on binding of oxygen to iron has been observed in crystal structures. We have determined structures of naphthalene dioxygenase that show a molecular oxygen species bound to the mononuclear iron in a side-on fashion. In a complex with substrate and dioxygen, the dioxygen molecule is lined up for an attack on the double bond of the aromatic substrate. The structures reported here provide the basis for a reaction mechanism and for the high stereospecificity of the reaction catalyzed by naphthalene dioxygenase.

Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron.,Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S Science. 2003 Feb 14;299(5609):1039-42. PMID:12586937[1]

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

See Also

References

  1. Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S. Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron. Science. 2003 Feb 14;299(5609):1039-42. PMID:12586937 doi:http://dx.doi.org/10.1126/science.1078020

1o7n, resolution 1.40Å

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