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| [[Image:1nu5.jpg|left|200px]]
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| {{Structure
| | ==Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme== |
| |PDB= 1nu5 |SIZE=350|CAPTION= <scene name='initialview01'>1nu5</scene>, resolution 1.95Å
| | <StructureSection load='1nu5' size='340' side='right'caption='[[1nu5]], [[Resolution|resolution]] 1.95Å' scene=''> |
| |SITE=
| | == Structural highlights == |
| |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
| | <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> |
| |ACTIVITY= <span class='plainlinks'>[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] </span>
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
| |GENE= | | <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> |
| |DOMAIN=
| | <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> |
| |RELATEDENTRY=
| | </table> |
| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nu5 OCA], [http://www.ebi.ac.uk/pdbsum/1nu5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nu5 RCSB]</span>
| | == Function == |
| }}
| | [https://www.uniprot.org/uniprot/TCBD_PSESQ TCBD_PSESQ] |
| | == 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/nu/1nu5_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=1nu5 ConSurf]. |
| | <div style="clear:both"></div> |
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| '''Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme'''
| | ==See Also== |
| | | *[[Muconate cycloisomerase|Muconate cycloisomerase]] |
| | | __TOC__ |
| ==Overview==
| | </StructureSection> |
| 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.
| | [[Category: Large Structures]] |
| | | [[Category: Pseudomonas sp. P51]] |
| ==About this Structure== | | [[Category: Goldman A]] |
| 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].
| | [[Category: Kajander T]] |
| | | [[Category: Lehtio L]] |
| ==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]] | |
| [[Category: Pseudomonas sp.]] | |
| [[Category: Single protein]]
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| [[Category: Goldman, A.]] | |
| [[Category: Kajander, T.]] | |
| [[Category: Lehtio, L.]] | |
| [[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 Sun Mar 30 22:35:41 2008''
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