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New page: left|200px<br /><applet load="1jof" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jof, resolution 2.5Å" /> '''Neurospora crassa 3-c...
 
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[[Image:1jof.jpg|left|200px]]<br /><applet load="1jof" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1jof, resolution 2.5&Aring;" />
'''Neurospora crassa 3-carboxy-cis,cis-mucoante lactonizing enzyme'''<br />


==Overview==
==Neurospora crassa 3-carboxy-cis,cis-mucoante lactonizing enzyme==
Muconate lactonizing enzymes (MLEs) convert cis,cis-muconates to, muconolactones in microbes as part of the beta-ketoadipate pathway; some, also dehalogenate muconate derivatives of xenobiotic haloaromatics. There, are three different MLE classes unrelated by evolution. We present the, X-ray structure of a eukaryotic MLE, Neurospora crassa, 3-carboxy-cis,cis-muconate lactonizing enzyme (NcCMLE) at 2.5 A, resolution, with a seven-bladed beta propeller fold. It is related neither, to bacterial MLEs nor to other beta propeller enzymes, but is structurally, similar to the G protein beta subunit. It reveals a novel, metal-independent cycloisomerase motif unlike the bacterial metal cofactor, MLEs. Together, the bacterial MLEs and NcCMLE structures comprise a, striking structural example of functional convergence in enzymes for, 1,2-addition-elimination of carboxylic acids. NcCMLE and bacterial MLEs, may enhance the reaction rate differently: the former by electrophilic, catalysis and the latter by electrostatic stabilization of the enolate.
<StructureSection load='1jof' size='340' side='right'caption='[[1jof]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jof]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JOF 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PIN:PIPERAZINE-N,N-BIS(2-ETHANESULFONIC+ACID)'>PIN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1jof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jof OCA], [https://pdbe.org/1jof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jof RCSB], [https://www.ebi.ac.uk/pdbsum/1jof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jof ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CMLE_NEUCR CMLE_NEUCR] Catalyzes a syn cycloisomerization. Also possesses mle activity.
== 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/jo/1jof_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=1jof ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1JOF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa] with SO4, PIN and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carboxy-cis,cis-muconate_cyclase Carboxy-cis,cis-muconate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.5 5.5.1.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JOF OCA].
*[[Muconate cycloisomerase|Muconate cycloisomerase]]
 
__TOC__
==Reference==
</StructureSection>
The structure of Neurospora crassa 3-carboxy-cis,cis-muconate lactonizing enzyme, a beta propeller cycloisomerase., Kajander T, Merckel MC, Thompson A, Deacon AM, Mazur P, Kozarich JW, Goldman A, Structure. 2002 Apr;10(4):483-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11937053 11937053]
[[Category: Large Structures]]
[[Category: Carboxy-cis,cis-muconate cyclase]]
[[Category: Neurospora crassa]]
[[Category: Neurospora crassa]]
[[Category: Single protein]]
[[Category: Deacon AM]]
[[Category: Deacon, A.M.]]
[[Category: Goldman A]]
[[Category: Goldman, A.]]
[[Category: Kajander T]]
[[Category: Kajander, T.]]
[[Category: Kozarich JW]]
[[Category: Kozarich, J.W.]]
[[Category: Mazur P]]
[[Category: Mazur, P.]]
[[Category: Merckel MC]]
[[Category: Merckel, M.C.]]
[[Category: Thompson A]]
[[Category: Thompson, A.]]
[[Category: BME]]
[[Category: PIN]]
[[Category: SO4]]
[[Category: beta-propeller]]
[[Category: homotetramer]]
[[Category: semet-protein]]
 
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