1lgt
From Proteopedia
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- | [[ | + | ==CRYSTAL STRUCTURE OF 2,3-DIHYDROXYBIPHENYL 1,2-DIOXYGENASE (DHBD) COMPLEXED WITH 2'-Cl DIHYDROXYBIPHENYL (DHB)== |
+ | <StructureSection load='1lgt' size='340' side='right' caption='[[1lgt]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1lgt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Burxl Burxl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LGT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LGT FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BP3:2-CHLORO-BIPHENYL-2,3-DIOL'>BP3</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1han|1han]], [[1lkd|1lkd]], [[1kmy|1kmy]], [[1knd|1knd]], [[1knf|1knf]]</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Biphenyl-2,3-diol_1,2-dioxygenase Biphenyl-2,3-diol 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.39 1.13.11.39] </span></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lgt OCA], [http://pdbe.org/1lgt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lgt RCSB], [http://www.ebi.ac.uk/pdbsum/1lgt PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/BPHC_BURXL BPHC_BURXL]] Shows a preference for catechols with groups immediately adjacent to the hydroxyl substituents. | ||
+ | == 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/lg/1lgt_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=1lgt ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The microbial degradation of polychlorinated biphenyls (PCBs) provides the potential to destroy these widespread, toxic and persistent environmental pollutants. For example, the four-step upper bph pathway transforms some of the more than 100 different PCBs found in commercial mixtures and is being engineered for more effective PCB degradation. In the critical third step of this pathway, 2,3-dihydroxybiphenyl (DHB) 1,2-dioxygenase (DHBD; EC 1.13.11.39) catalyzes aromatic ring cleavage. Here we demonstrate that ortho-chlorinated PCB metabolites strongly inhibit DHBD, promote its suicide inactivation and interfere with the degradation of other compounds. For example, k(cat)(app) for 2',6'-diCl DHB was reduced by a factor of approximately 7,000 relative to DHB, and it bound with sufficient affinity to competitively inhibit DHB cleavage at nanomolar concentrations. Crystal structures of two complexes of DHBD with ortho-chlorinated metabolites at 1.7 A resolution reveal an explanation for these phenomena, which have important implications for bioremediation strategies. | ||
- | + | Identification and analysis of a bottleneck in PCB biodegradation.,Dai S, Vaillancourt FH, Maaroufi H, Drouin NM, Neau DB, Snieckus V, Bolin JT, Eltis LD Nat Struct Biol. 2002 Dec;9(12):934-9. PMID:12415290<ref>PMID:12415290</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
+ | <div class="pdbe-citations 1lgt" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | == | + | *[[Dioxygenase|Dioxygenase]] |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | ||
- | == | + | |
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[[Category: Biphenyl-2,3-diol 1,2-dioxygenase]] | [[Category: Biphenyl-2,3-diol 1,2-dioxygenase]] | ||
- | [[Category: | + | [[Category: Burxl]] |
- | + | [[Category: Bolin, J T]] | |
- | [[Category: Bolin, J T | + | [[Category: Dai, S]] |
- | [[Category: Dai, S | + | |
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[[Category: 3-dihydroxybiphenyl]] | [[Category: 3-dihydroxybiphenyl]] | ||
- | [[Category: | + | [[Category: Anaerobic]] |
- | [[Category: | + | [[Category: Extradiol dioxygenase]] |
- | [[Category: | + | [[Category: Non-heme iron]] |
- | [[Category: | + | [[Category: Oxidoreductase]] |
- | + | [[Category: Pcb biodegradation]] | |
- | + |
Current revision
CRYSTAL STRUCTURE OF 2,3-DIHYDROXYBIPHENYL 1,2-DIOXYGENASE (DHBD) COMPLEXED WITH 2'-Cl DIHYDROXYBIPHENYL (DHB)
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