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1eeh

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(New page: 200px<br /><applet load="1eeh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eeh, resolution 1.9&Aring;" /> '''UDP-N-ACETYLMURAMOYL-...)
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[[Image:1eeh.gif|left|200px]]<br /><applet load="1eeh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1eeh, resolution 1.9&Aring;" />
 
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'''UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE'''<br />
 
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==Overview==
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==UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE==
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UDP-N-acetylmuramoyl-l-alanine:d-glutamate (MurD) ligase catalyses the, addition of d-glutamate to the nucleotide precursor, UDP-N-acetylmuramoyl-l-alanine (UMA). The crystal structures of, Escherichia coli in the substrate-free form and MurD complexed with UMA, have been determined at 2.4 A and 1.88 A resolution, respectively. The, MurD structure comprises three domains each of a topology reminiscent of, nucleotide-binding folds. In the two structures the C-terminal domain, undergoes a large rigid-body rotation away from the N-terminal and central, domains. These two "open" structures were compared with the four published, "closed" structures of MurD. In addition the comparison reveals which, regions are affected by the binding of UMA, ATP and d-Glu. Also we compare, and discuss two structurally characterized enzymes which belong to the, same ligase superfamily: MurD and folylpolyglutamate synthetase (FGS). The, analysis allows the identification of key residues involved in the, reaction mechanism of FGS. The determination of the two "open", conformation structures represents a new step towards the complete, elucidation of the enzymatic mechanism of the MurD ligase.
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<StructureSection load='1eeh' size='340' side='right'caption='[[1eeh]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1eeh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EEH FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UMA:URIDINE-5-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE'>UMA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eeh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eeh OCA], [https://pdbe.org/1eeh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eeh RCSB], [https://www.ebi.ac.uk/pdbsum/1eeh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eeh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MURD_ECOLI MURD_ECOLI] Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).[HAMAP-Rule:MF_00639]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ee/1eeh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1eeh ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1EEH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with UMA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylmuramoyl-L-alanine--D-glutamate_ligase UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.9 6.3.2.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EEH OCA].
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*[[Mur ligase|Mur ligase]]
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__TOC__
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==Reference==
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</StructureSection>
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"Open" structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase., Bertrand JA, Fanchon E, Martin L, Chantalat L, Auger G, Blanot D, van Heijenoort J, Dideberg O, J Mol Biol. 2000 Sep 1;301(5):1257-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10966819 10966819]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase]]
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[[Category: Auger G]]
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[[Category: Auger, G.]]
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[[Category: Bertrand JA]]
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[[Category: Bertrand, J.A.]]
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[[Category: Blanot D]]
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[[Category: Blanot, D.]]
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[[Category: Chantalat L]]
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[[Category: Chantalat, L.]]
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[[Category: Dideberg O]]
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[[Category: Dideberg, O.]]
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[[Category: Fanchon E]]
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[[Category: Fanchon, E.]]
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[[Category: Martin L]]
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[[Category: Heijenoort, J.van.]]
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[[Category: Van Heijenoort J]]
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[[Category: Martin, L.]]
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[[Category: UMA]]
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[[Category: adp-forming enzyme]]
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[[Category: ligase]]
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[[Category: murd]]
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[[Category: peptidoglycan synthesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:56:37 2007''
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Current revision

UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE

PDB ID 1eeh

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