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| | <StructureSection load='2jfh' size='340' side='right'caption='[[2jfh]], [[Resolution|resolution]] 1.97Å' scene=''> | | <StructureSection load='2jfh' size='340' side='right'caption='[[2jfh]], [[Resolution|resolution]] 1.97Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jfh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JFH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JFH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jfh]] 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=2JFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JFH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LK1:N-[(6-BUTOXYNAPHTHALEN-2-YL)SULFONYL]-L-GLUTAMIC+ACID'>LK1</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.97Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr> | + | <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=LK1:N-[(6-BUTOXYNAPHTHALEN-2-YL)SULFONYL]-L-GLUTAMIC+ACID'>LK1</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e0d|1e0d]], [[1eeh|1eeh]], [[1uag|1uag]], [[2uag|2uag]], [[3uag|3uag]], [[4uag|4uag]], [[2jff|2jff]], [[2jfg|2jfg]]</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=2jfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jfh OCA], [https://pdbe.org/2jfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jfh RCSB], [https://www.ebi.ac.uk/pdbsum/2jfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jfh ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=2jfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jfh OCA], [http://pdbe.org/2jfh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jfh RCSB], [http://www.ebi.ac.uk/pdbsum/2jfh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jfh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase]]
| + | [[Category: Blanot D]] |
| - | [[Category: Blanot, D]] | + | [[Category: Contreras-Martel C]] |
| - | [[Category: Contreras-Martel, C]] | + | [[Category: Dessen A]] |
| - | [[Category: Dessen, A]] | + | [[Category: Gobec S]] |
| - | [[Category: Gobec, S]] | + | [[Category: Herve M]] |
| - | [[Category: Herve, M]] | + | [[Category: Humljan J]] |
| - | [[Category: Humljan, J]] | + | [[Category: Kotnik M]] |
| - | [[Category: Kotnik, M]] | + | [[Category: Kristan K]] |
| - | [[Category: Kristan, K]] | + | [[Category: Oblak M]] |
| - | [[Category: Oblak, M]] | + | [[Category: Solmajer T]] |
| - | [[Category: Solmajer, T]] | + | [[Category: Urleb U]] |
| - | [[Category: Urleb, U]] | + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Cell division]]
| + | |
| - | [[Category: Cell shape]]
| + | |
| - | [[Category: Cell wall]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Murd ligase]]
| + | |
| - | [[Category: Murd-inhibitor complex]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Peptidoglycan synthesis]]
| + | |
| - | [[Category: Sulfonamide inhibitor]]
| + | |
| Structural highlights
Function
MURD_ECOLI Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).[HAMAP-Rule:MF_00639]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Mur ligases play an essential role in the intracellular biosynthesis of bacterial peptidoglycan, the main component of the bacterial cell wall, and represent attractive targets for the design of novel antibacterials. UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase (MurD) catalyses the addition of D-glutamic acid to the cytoplasmic intermediate UDP-N-acetylmuramoyl-L-alanine (UMA) and is the second in the series of Mur ligases. MurD ligase is highly stereospecific for its substrate, D-glutamic acid (D-Glu). Here, we report the high resolution crystal structures of MurD in complexes with two novel inhibitors designed to mimic the transition state of the reaction, which contain either the D-Glu or the L-Glu moiety. The binding modes of N-sulfonyl-D-Glu and N-sulfonyl-L-Glu derivatives were also characterised kinetically. The results of this study represent an excellent starting point for further development of novel inhibitors of this enzyme.
Structural and functional characterization of enantiomeric glutamic acid derivatives as potential transition state analogue inhibitors of MurD ligase.,Kotnik M, Humljan J, Contreras-Martel C, Oblak M, Kristan K, Herve M, Blanot D, Urleb U, Gobec S, Dessen A, Solmajer T J Mol Biol. 2007 Jun 29;370(1):107-15. Epub 2007 May 4. PMID:17507028[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kotnik M, Humljan J, Contreras-Martel C, Oblak M, Kristan K, Herve M, Blanot D, Urleb U, Gobec S, Dessen A, Solmajer T. Structural and functional characterization of enantiomeric glutamic acid derivatives as potential transition state analogue inhibitors of MurD ligase. J Mol Biol. 2007 Jun 29;370(1):107-15. Epub 2007 May 4. PMID:17507028 doi:http://dx.doi.org/10.1016/j.jmb.2007.04.048
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