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1uag

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(New page: 200px<br /><applet load="1uag" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uag, resolution 1.95&Aring;" /> '''UDP-N-ACETYLMURAMOYL...)
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[[Image:1uag.gif|left|200px]]<br /><applet load="1uag" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1uag, resolution 1.95&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 ligase (MurD) is a cytoplasmic, enzyme involved in the biosynthesis of peptidoglycan which catalyzes the, addition of D-glutamate to the nucleotide precursor, UDP-N-acetylmuramoyl-L-alanine (UMA). The crystal structure of MurD in the, presence of its substrate UMA has been solved to 1.9 A resolution. Phase, information was obtained from multiple anomalous dispersion using the, K-shell edge of selenium in combination with multiple isomorphous, replacement. The structure comprises three domains of topology each, reminiscent of nucleotide-binding folds: the N- and C-terminal domains are, consistent with the dinucleotide-binding fold called the Rossmann fold, and the central domain with the mononucleotide-binding fold also observed, in the GTPase family. The structure reveals the binding site of the, substrate UMA, and comparison with known NTP complexes allows the, identification of residues interacting with ATP. The study describes the, first structure of the UDP-N-acetylmuramoyl-peptide ligase family.
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<StructureSection load='1uag' size='340' side='right'caption='[[1uag]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1uag]] 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=1UAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UAG 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]] 1.95&#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=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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=1uag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uag OCA], [https://pdbe.org/1uag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uag RCSB], [https://www.ebi.ac.uk/pdbsum/1uag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uag 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/ua/1uag_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1uag ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase (MurD) is a cytoplasmic enzyme involved in the biosynthesis of peptidoglycan which catalyzes the addition of D-glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). The crystal structure of MurD in the presence of its substrate UMA has been solved to 1.9 A resolution. Phase information was obtained from multiple anomalous dispersion using the K-shell edge of selenium in combination with multiple isomorphous replacement. The structure comprises three domains of topology each reminiscent of nucleotide-binding folds: the N- and C-terminal domains are consistent with the dinucleotide-binding fold called the Rossmann fold, and the central domain with the mononucleotide-binding fold also observed in the GTPase family. The structure reveals the binding site of the substrate UMA, and comparison with known NTP complexes allows the identification of residues interacting with ATP. The study describes the first structure of the UDP-N-acetylmuramoyl-peptide ligase family.
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==About this Structure==
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Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli.,Bertrand JA, Auger G, Fanchon E, Martin L, Blanot D, van Heijenoort J, Dideberg O EMBO J. 1997 Jun 16;16(12):3416-25. PMID:9218784<ref>PMID:9218784</ref>
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1UAG 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 SO4 and UMA as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1UAG OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli., Bertrand JA, Auger G, Fanchon E, Martin L, Blanot D, van Heijenoort J, Dideberg O, EMBO J. 1997 Jun 16;16(12):3416-25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9218784 9218784]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 1uag" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase]]
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[[Category: Bertrand, J.]]
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[[Category: Dideberg, O.]]
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[[Category: Fanchon, E.]]
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[[Category: SO4]]
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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 Wed Nov 21 03:57:45 2007''
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==See Also==
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*[[Mur ligase|Mur ligase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Bertrand J]]
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[[Category: Dideberg O]]
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[[Category: Fanchon E]]

Current revision

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

PDB ID 1uag

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