2zad: Difference between revisions

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==Crystal Structure of Muconate Cycloisomerase from Thermotoga maritima MSB8==
==Crystal Structure of Muconate Cycloisomerase from Thermotoga maritima MSB8==
<StructureSection load='2zad' size='340' side='right' caption='[[2zad]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='2zad' size='340' side='right' caption='[[2zad]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Muconate_cycloisomerase Muconate cycloisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.1 5.5.1.1] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Muconate_cycloisomerase Muconate cycloisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.1 5.5.1.1] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zad OCA], [http://pdbe.org/2zad PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zad RCSB], [http://www.ebi.ac.uk/pdbsum/2zad PDBsum], [http://www.topsan.org/Proteins/RSGI/2zad TOPSAN]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zad OCA], [http://pdbe.org/2zad PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zad RCSB], [http://www.ebi.ac.uk/pdbsum/2zad PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zad ProSAT], [http://www.topsan.org/Proteins/RSGI/2zad TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/za/2zad_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/za/2zad_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>

Revision as of 12:24, 17 October 2018

Crystal Structure of Muconate Cycloisomerase from Thermotoga maritima MSB8Crystal Structure of Muconate Cycloisomerase from Thermotoga maritima MSB8

Structural highlights

2zad is a 4 chain structure with sequence from Thema. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
NonStd Res:
Activity:Muconate cycloisomerase, with EC number 5.5.1.1
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[AEEP_THEMA] Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-Glu and has probably a role in the metabolism of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the reverse reaction and the epimerization of a broad range of other dipeptides; is most efficient with L-Ala-D/L-Phe, L-Ala-D/L-Tyr, and L-Ala-D/L-His.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Kalyanaraman C, Imker HJ, Fedorov AA, Fedorov EV, Glasner ME, Babbitt PC, Almo SC, Gerlt JA, Jacobson MP. Discovery of a dipeptide epimerase enzymatic function guided by homology modeling and virtual screening. Structure. 2008 Nov;16(11):1668-77. PMID:19000819 doi:S0969-2126(08)00371-7

2zad, resolution 1.60Å

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OCA