1ejd: Difference between revisions

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-[[Image:1ejd.gif|left|200px]]<br /><applet load="1ejd" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1ejd, resolution 1.55&Aring;" />
-'''CRYSTAL STRUCTURE OF UNLIGANDED MURA (TYPE1)'''<br />
-==Overview==
+==Crystal structure of unliganded mura (type1)==
-MurA, an essential enzyme for the synthesis of the bacterial cell wall, follows an induced-fit mechanism. Upon substrate binding, the active site, forms in the interdomain cleft, involving movements of the two domains of, the protein and a reorientation of the loop Pro112-Pro121. We compare two, structures of un-liganded MurA from Enterobacter cloacae: a new, orthorhombic form, solved to 1.80 A resolution, and a monoclinic form, redetermined to 1.55 A resolution. In the monoclinic form, the loop, Pro112-Pro121 stretches into solvent, while in the new form it adopts a, winded conformation, thereby reducing solvent accessibility of the, critical residue Cys115. In the interdomain cleft a network of 27 common, water molecules has been identified, which partially shields negative, charges in the cleft and stabilizes the orientation of catalytically, crucial residues. This could support substrate binding and ease domain, movements. Near the hinge region an isoaspartyl residue has been, recognized, which is the product of post-translational modification of the, genetically encoded Asn67-Gly68. The homogeneous population with, L-isoaspartate in both structures suggests that the modification in, Enterobacter cloacae MurA is not a mere aging defect but rather the result, of a specific in vivo process.
+<StructureSection load='1ejd' size='340' side='right'caption='[[1ejd]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ejd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EJD 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]] 1.55&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HAI:CYCLOHEXYLAMMONIUM+ION'>HAI</scene>, <scene name='pdbligand=IAS:BETA-L-ASPARTIC+ACID'>IAS</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1ejd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ejd OCA], [https://pdbe.org/1ejd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ejd RCSB], [https://www.ebi.ac.uk/pdbsum/1ejd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ejd ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MURA_ENTCC MURA_ENTCC] Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic phosphomycin.
+== 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/ej/1ejd_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ejd ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+MurA, an essential enzyme for the synthesis of the bacterial cell wall, follows an induced-fit mechanism. Upon substrate binding, the active site forms in the interdomain cleft, involving movements of the two domains of the protein and a reorientation of the loop Pro112-Pro121. We compare two structures of un-liganded MurA from Enterobacter cloacae: a new orthorhombic form, solved to 1.80 A resolution, and a monoclinic form, redetermined to 1.55 A resolution. In the monoclinic form, the loop Pro112-Pro121 stretches into solvent, while in the new form it adopts a winded conformation, thereby reducing solvent accessibility of the critical residue Cys115. In the interdomain cleft a network of 27 common water molecules has been identified, which partially shields negative charges in the cleft and stabilizes the orientation of catalytically crucial residues. This could support substrate binding and ease domain movements. Near the hinge region an isoaspartyl residue has been recognized, which is the product of post-translational modification of the genetically encoded Asn67-Gly68. The homogeneous population with L-isoaspartate in both structures suggests that the modification in Enterobacter cloacae MurA is not a mere aging defect but rather the result of a specific in vivo process.
-==About this Structure==
+Comparative X-ray analysis of the un-liganded fosfomycin-target murA.,Eschenburg S, Schonbrunn E Proteins. 2000 Aug 1;40(2):290-8. PMID:10842342<ref>PMID:10842342</ref>
-EJD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae] with PO4 and HAI as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_1-carboxyvinyltransferase UDP-N-acetylglucosamine 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.7 2.5.1.7] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EJD OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Comparative X-ray analysis of the un-liganded fosfomycin-target murA., Eschenburg S, Schonbrunn E, Proteins. 2000 Aug 1;40(2):290-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10842342 10842342]
+</div>
+<div class="pdbe-citations 1ejd" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Enoylpyruvate transferase 3D structures|Enoylpyruvate transferase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Enterobacter cloacae]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: UDP-N-acetylglucosamine 1-carboxyvinyltransferase]]
+[[Category: Eschenburg S]]
-[[Category: Eschenburg, S.]]
+[[Category: Schonbrunn E]]
-[[Category: Schonbrunn, E.]]
-[[Category: HAI]]
-[[Category: PO4]]
-[[Category: inside-out alpha/beta barrel]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:03:12 2007''