1fqt

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(New page: 200px<br /><applet load="1fqt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fqt, resolution 1.60&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1fqt.gif|left|200px]]<br /><applet load="1fqt" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fqt, resolution 1.60&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE RIESKE-TYPE FERREDOXIN ASSOCIATED WITH BIPHENYL DIOXYGENASE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE RIESKE-TYPE FERREDOXIN ASSOCIATED WITH BIPHENYL DIOXYGENASE==
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BACKGROUND: Ring-hydroxylating dioxygenases are multicomponent systems, that initiate biodegradation of aromatic compounds. Many dioxygenase, systems include Rieske-type ferredoxins with amino acid sequences and, redox properties remarkably different from the Rieske proteins of, proton-translocating respiratory and photosynthetic complexes. In the, latter, the [Fe2S2] clusters lie near the protein surface, operate at, potentials above +300 mV at pH 7, and express pH- and ionic, strength-dependent redox behavior. The reduction potentials of the, dioxygenase ferredoxins are approximately 150 mV and are pH-independent., These distinctions were predicted to arise from differences in the, exposure of the cluster and/or interactions of the histidine ligands., RESULTS: The crystal structure of BphF, the Rieske-type ferredoxin, associated with biphenyl dioxygenase, was determined by multiwavelength, anomalous diffraction and refined at 1.6 A resolution. The structure of, BphF was compared with other Rieske proteins at several levels. BphF has, the same two-domain fold as other Rieske proteins, but it lacks all, insertions that give the others unique structural features. The BphF Fe-S, cluster and its histidine ligands are exposed. However, the cluster has a, significantly different environment in that five fewer polar groups, interact strongly with the cluster sulfide or the cysteinyl ligands., CONCLUSIONS: BphF has structural features consistent with a minimal and, perhaps archetypical Rieske protein. Variations in redox potentials among, Rieske clusters appear to be largely the result of local electrostatic, interactions with protein partial charges. Moreover, it appears that the, redox-linked ionizations of the Rieske proteins from proton-translocating, complexes are also promoted by these electrostatic interactions.
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<StructureSection load='1fqt' size='340' side='right'caption='[[1fqt]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1fqt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paraburkholderia_xenovorans_LB400 Paraburkholderia xenovorans LB400]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQT FirstGlance]. <br>
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1FQT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia] with FES and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FQT OCA].
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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]] 1.6&#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=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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==Reference==
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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=1fqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fqt OCA], [https://pdbe.org/1fqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fqt RCSB], [https://www.ebi.ac.uk/pdbsum/1fqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fqt ProSAT]</span></td></tr>
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A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins., Colbert CL, Couture MM, Eltis LD, Bolin JT, Structure. 2000 Dec 15;8(12):1267-78. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11188691 11188691]
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</table>
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[[Category: Burkholderia cepacia]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/BPHF_PARXL BPHF_PARXL] This protein seems to be a 2Fe-2S ferredoxin.
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[[Category: Bolin, J.T.]]
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== Evolutionary Conservation ==
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[[Category: Colbert, C.L.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Couture, M.M.J.]]
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Check<jmol>
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[[Category: Eltis, L.D.]]
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<jmolCheckbox>
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[[Category: FES]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/1fqt_consurf.spt"</scriptWhenChecked>
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[[Category: GOL]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: 2fe-2s cluster]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: beta sandwich]]
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</jmolCheckbox>
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[[Category: rieske-type ferredoxin]]
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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=1fqt ConSurf].
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<div style="clear:both"></div>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:10:24 2007''
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Paraburkholderia xenovorans LB400]]
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[[Category: Bolin JT]]
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[[Category: Colbert CL]]
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[[Category: Couture MM-J]]
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[[Category: Eltis LD]]

Current revision

CRYSTAL STRUCTURE OF THE RIESKE-TYPE FERREDOXIN ASSOCIATED WITH BIPHENYL DIOXYGENASE

PDB ID 1fqt

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