1jof
From Proteopedia
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<StructureSection load='1jof' size='340' side='right'caption='[[1jof]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1jof' size='340' side='right'caption='[[1jof]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1jof]] is a 8 chain structure with sequence from [ | + | <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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
- | <tr id=' | + | <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> | |
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- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/CMLE_NEUCR CMLE_NEUCR] Catalyzes a syn cycloisomerization. Also possesses mle activity. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1jof ConSurf]. | </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> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | 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. | ||
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- | 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:11937053<ref>PMID:11937053</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1jof" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Muconate cycloisomerase|Muconate cycloisomerase]] | *[[Muconate cycloisomerase|Muconate cycloisomerase]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Carboxy-cis,cis-muconate cyclase]] | ||
- | [[Category: Chrysonilia crassa]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Deacon | + | [[Category: Neurospora crassa]] |
- | [[Category: Goldman | + | [[Category: Deacon AM]] |
- | [[Category: Kajander | + | [[Category: Goldman A]] |
- | [[Category: Kozarich | + | [[Category: Kajander T]] |
- | [[Category: Mazur | + | [[Category: Kozarich JW]] |
- | [[Category: Merckel | + | [[Category: Mazur P]] |
- | [[Category: Thompson | + | [[Category: Merckel MC]] |
- | + | [[Category: Thompson A]] | |
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Current revision
Neurospora crassa 3-carboxy-cis,cis-mucoante lactonizing enzyme
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