1o7n: Difference between revisions

No edit summary
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1o7n.jpg|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/Naphthalene_1,2-dioxygenase Naphthalene 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.12.12 1.14.12.12] Known structural/functional Site: <scene name='pdbsite=AC1:Fe Binding Site For Chain A'>AC1</scene>. 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: Naphthalene 1,2-dioxygenase]]
<div class="pdbe-citations 1o7n" style="background-color:#fffaf0;"></div>
[[Category: Protein complex]]
 
==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 Tue Dec 18 16:58:49 2007''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA