2ckf

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[[Image:2ckf.gif|left|200px]]<br />
 
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<applet load="2ckf" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ckf, resolution 1.85&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE TERMINAL COMPONENT OF THE PAH-HYDROXYLATING DIOXYGENASE FROM SPHINGOMONAS SP CHY-1'''<br />
 
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==Overview==
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==Crystal Structure of the Terminal Component of the PAH-hydroxylating Dioxygenase from Sphingomonas sp CHY-1==
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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.
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<StructureSection load='2ckf' size='340' side='right'caption='[[2ckf]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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]] 1.85&#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=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
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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=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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q65AT1_9SPHN Q65AT1_9SPHN]
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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/ck/2ckf_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=2ckf ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2CKF is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Sphingomonas_sp._chy-1 Sphingomonas sp. chy-1]] with FE and FES as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CKF OCA]].
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*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17157819 17157819]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Sphingomonas sp. CHY-1]]
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[[Category: Sphingomonas sp. chy-1]]
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[[Category: Jakoncic J]]
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[[Category: Jakoncic, J.]]
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[[Category: Jouanneau Y]]
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[[Category: Jouanneau, Y.]]
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[[Category: Meyer C]]
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[[Category: Meyer, C.]]
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[[Category: Stojanoff V]]
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[[Category: Stojanoff, V.]]
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[[Category: FE]]
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[[Category: FES]]
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[[Category: high-molecular-weight polycyclic aromatic hydrocarbons]]
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[[Category: oxidoreductase]]
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[[Category: pyrene dioxygenase]]
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[[Category: rieske non heme iron dioxygenase]]
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[[Category: ring-hydroxylating dioxygenase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:36:11 2007''
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Current revision

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

PDB ID 2ckf

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