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[[Image:2ckf.jpg|left|200px]]
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{{STRUCTURE_2ckf|  PDB=2ckf  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF THE TERMINAL COMPONENT OF THE PAH-HYDROXYLATING DIOXYGENASE FROM SPHINGOMONAS SP CHY-1'''


==Crystal Structure of the Terminal Component of the PAH-hydroxylating Dioxygenase from Sphingomonas sp CHY-1==
<StructureSection load='2ckf' size='340' side='right'caption='[[2ckf]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ckf]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_sp._CHY-1 Sphingomonas sp. CHY-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CKF 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]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=2ckf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ckf OCA], [https://pdbe.org/2ckf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ckf RCSB], [https://www.ebi.ac.uk/pdbsum/2ckf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ckf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q65AT1_9SPHN Q65AT1_9SPHN]
== 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/ck/2ckf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2ckf ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ring-hydroxylating dioxygenases are multicomponent bacterial enzymes that catalyze the first step in the oxidative degradation of aromatic hydrocarbons. The dioxygenase from Sphingomonas CHY-1 is unique in that it can oxidize a wide range of polycyclic aromatic hydrocarbons (PAHs). With a crystal structure similar to that of the seven other known dioxygenases, its catalytic domain features the largest hydrophobic substrate binding cavity characterized so far. Molecular modeling studies indicated that the catalytic cavity is large enough to accommodate a five-ring benzo[a]pyrene molecule. The predicted positions of this and other PAHs in the substrate binding pocket are consistent with the product regio- and stereo-selectivity of the enzyme.


==Overview==
The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1.,Jakoncic J, Jouanneau Y, Meyer C, Stojanoff V Biochem Biophys Res Commun. 2007 Jan 26;352(4):861-6. Epub 2006 Dec 4. PMID:17157819<ref>PMID:17157819</ref>
Ring-hydroxylating dioxygenases are multicomponent bacterial enzymes that catalyze the first step in the oxidative degradation of aromatic hydrocarbons. The dioxygenase from Sphingomonas CHY-1 is unique in that it can oxidize a wide range of polycyclic aromatic hydrocarbons (PAHs). With a crystal structure similar to that of the seven other known dioxygenases, its catalytic domain features the largest hydrophobic substrate binding cavity characterized so far. Molecular modeling studies indicated that the catalytic cavity is large enough to accommodate a five-ring benzo[a]pyrene molecule. The predicted positions of this and other PAHs in the substrate binding pocket are consistent with the product regio- and stereo-selectivity of the enzyme.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2CKF is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKF OCA].
</div>
<div class="pdbe-citations 2ckf" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1., Jakoncic J, Jouanneau Y, Meyer C, Stojanoff V, Biochem Biophys Res Commun. 2007 Jan 26;352(4):861-6. Epub 2006 Dec 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17157819 17157819]
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
[[Category: Bacteria]]
== References ==
[[Category: Protein complex]]
<references/>
[[Category: Jakoncic, J.]]
__TOC__
[[Category: Jouanneau, Y.]]
</StructureSection>
[[Category: Meyer, C.]]
[[Category: Large Structures]]
[[Category: Stojanoff, V.]]
[[Category: Sphingomonas sp. CHY-1]]
[[Category: High-molecular-weight polycyclic aromatic hydrocarbon]]
[[Category: Jakoncic J]]
[[Category: Oxidoreductase]]
[[Category: Jouanneau Y]]
[[Category: Pyrene dioxygenase]]
[[Category: Meyer C]]
[[Category: Rieske non heme iron dioxygenase]]
[[Category: Stojanoff V]]
[[Category: Ring-hydroxylating dioxygenase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 22:21:15 2008''

Latest revision as of 17:22, 8 September 2026

Crystal Structure of the Terminal Component of the PAH-hydroxylating Dioxygenase from Sphingomonas sp CHY-1

2ckf, resolution 1.85Å

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