1nu5

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[[Image:1nu5.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme==
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|PDB= 1nu5 |SIZE=350|CAPTION= <scene name='initialview01'>1nu5</scene>, resolution 1.95&Aring;
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<StructureSection load='1nu5' size='340' side='right'caption='[[1nu5]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene>
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<table><tr><td colspan='2'>[[1nu5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._P51 Pseudomonas sp. P51]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NU5 FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Chloromuconate_cycloisomerase Chloromuconate cycloisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.7 5.5.1.7]
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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]] 1.95&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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}}
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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=1nu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nu5 OCA], [https://pdbe.org/1nu5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nu5 RCSB], [https://www.ebi.ac.uk/pdbsum/1nu5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nu5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TCBD_PSESQ TCBD_PSESQ]
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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/nu/1nu5_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=1nu5 ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme'''
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==See Also==
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*[[Muconate cycloisomerase|Muconate cycloisomerase]]
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__TOC__
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==Overview==
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</StructureSection>
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Bacterial muconate lactonizing enzymes (MLEs) catalyze the conversion of cis,cis-muconate as a part of the beta-ketoadipate pathway, and some MLEs are also able to dehalogenate chlorinated muconates (Cl-MLEs). The basis for the Cl-MLEs dehalogenating activity is still unclear. To further elucidate the differences between MLEs and Cl-MLEs, we have solved the structure of Pseudomonas P51 Cl-MLE at 1.95 A resolution. Comparison of Pseudomonas MLE and Cl-MLE structures reveals the presence of a large cavity in the Cl-MLEs. The cavity may be related to conformational changes on substrate binding in Cl-MLEs, at Gly52. Site-directed mutagenesis on Pseudomonas MLE core positions to the equivalent Cl-MLE residues showed that the variant Thr52Gly was rather inactive, whereas the Thr52Gly-Phe103Ser variant had regained part of the activity. These residues form a hydrogen bond in the Cl-MLEs. The Cl-MLE structure, as a result of the Thr-to-Gly change, is more flexible than MLE: As a mobile loop closes over the active site, a conformational change at Gly52 is observed in Cl-MLEs. The loose packing and structural motions in Cl-MLE may be required for the rotation of the lactone ring in the active site necessary for the dehalogenating activity of Cl-MLEs. Furthermore, we also suggest that differences in the active site mobile loop sequence between MLEs and Cl-MLEs result in lower active site polarity in Cl-MLEs, possibly affecting catalysis. These changes could result in slower product release from Cl-MLEs and make it a better enzyme for dehalogenation of substrate.
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[[Category: Large Structures]]
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[[Category: Pseudomonas sp. P51]]
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==About this Structure==
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[[Category: Goldman A]]
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1NU5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NU5 OCA].
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[[Category: Kajander T]]
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[[Category: Lehtio L]]
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==Reference==
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The structure of Pseudomonas P51 Cl-muconate lactonizing enzyme: co-evolution of structure and dynamics with the dehalogenation function., Kajander T, Lehtio L, Schlomann M, Goldman A, Protein Sci. 2003 Sep;12(9):1855-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12930985 12930985]
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[[Category: Chloromuconate cycloisomerase]]
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[[Category: Pseudomonas sp.]]
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[[Category: Single protein]]
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[[Category: Goldman, A.]]
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[[Category: Kajander, T.]]
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[[Category: Lehtio, L.]]
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[[Category: MN]]
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[[Category: dehalogenation]]
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[[Category: enzyme]]
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[[Category: muconate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:01:43 2008''
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Current revision

Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme

PDB ID 1nu5

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