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[[Image:1nu5.jpg|left|200px]]<br /><applet load="1nu5" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nu5, resolution 1.95&Aring;" />
'''Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme'''<br />


==Overview==
==Crystal structure of Pseudomonas sp. P51 Chloromuconate lactonizing enzyme==
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.
<StructureSection load='1nu5' size='340' side='right'caption='[[1nu5]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== 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>


==About this Structure==
==See Also==
1NU5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NU5 OCA].
*[[Muconate cycloisomerase|Muconate cycloisomerase]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12930985 12930985]
[[Category: Large Structures]]
[[Category: Chloromuconate cycloisomerase]]
[[Category: Pseudomonas sp. P51]]
[[Category: Pseudomonas sp.]]
[[Category: Goldman A]]
[[Category: Single protein]]
[[Category: Kajander T]]
[[Category: Goldman, A.]]
[[Category: Lehtio L]]
[[Category: Kajander, T.]]
[[Category: Lehtio, L.]]
[[Category: MN]]
[[Category: dehalogenation]]
[[Category: enzyme]]
[[Category: muconate]]
 
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Retrieved from "https://proteopedia.org/1nu5"