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==CRYSTAL STRUCTURE OF MURD LIGASE FROM ESCHERICHIA COLI== | |||
<StructureSection load='5a5e' size='340' side='right' caption='[[5a5e]], [[Resolution|resolution]] 1.84Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5a5e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A5E FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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">[[5a5f|5a5f]]</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=5a5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a5e OCA], [http://pdbe.org/5a5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a5e RCSB], [http://www.ebi.ac.uk/pdbsum/5a5e PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The biosynthetic pathway of peptidoglycan, an essential component of bacterial cell wall, is a well-recognized target for antibiotic development. Peptidoglycan precursors are synthesized in the bacterial cytosol by various enzymes including the ATP-hydrolyzing Mur ligases, which catalyze the stepwise addition of amino acids to a UDP-MurNAc precursor to yield UDP-MurNAc-pentapeptide. MurD catalyzes the addition of D-glutamic acid to UDP-MurNAc-L-Ala in the presence of ATP; structural and biochemical studies have suggested the binding of the substrates with an ordered kinetic mechanism in which ligand binding inevitably closes the active site. In this work, we challenge this assumption by reporting the crystal structures of intermediate forms of MurD either in the absence of ligands or in the presence of small molecules. A detailed analysis provides insight into the events that lead to the closure of MurD and reveals that minor structural modifications contribute to major overall conformation alterations. These novel insights will be instrumental in the development of new potential antibiotics designed to target the peptidoglycan biosynthetic pathway. | |||
Crystallographic Study of Peptidoglycan Biosynthesis Enzyme MurD: Domain Movement Revisited.,Sink R, Kotnik M, Zega A, Barreteau H, Gobec S, Blanot D, Dessen A, Contreras-Martel C PLoS One. 2016 Mar 31;11(3):e0152075. doi: 10.1371/journal.pone.0152075., eCollection 2016. PMID:27031227<ref>PMID:27031227</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5a5e" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase]] | |||
[[Category: Barreteau, H]] | |||
[[Category: Blanot, D]] | |||
[[Category: Contreras-Martel, C]] | |||
[[Category: Dessen, A]] | |||
[[Category: Gobec, S]] | [[Category: Gobec, S]] | ||
[[Category: Kotnik, M]] | [[Category: Kotnik, M]] | ||
[[Category: Sink, R]] | [[Category: Sink, R]] | ||
[[Category: Zega, A]] | [[Category: Zega, A]] | ||
[[Category: | [[Category: Adp-forming enzyme]] | ||
[[Category: Atp- binding]] | |||
[[Category: Cell cycle]] | |||
[[Category: Cell division]] | |||
[[Category: Cell shape]] | |||
[[Category: Cell wall]] | |||
[[Category: Conformation]] | |||
[[Category: Ligand]] | |||
[[Category: Ligase]] | |||
[[Category: Nucleotide-binding]] | |||
[[Category: Peptidoglycan synthesis]] | |||
Revision as of 14:22, 12 May 2016
CRYSTAL STRUCTURE OF MURD LIGASE FROM ESCHERICHIA COLICRYSTAL STRUCTURE OF MURD LIGASE FROM ESCHERICHIA COLI
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] Publication Abstract from PubMedThe biosynthetic pathway of peptidoglycan, an essential component of bacterial cell wall, is a well-recognized target for antibiotic development. Peptidoglycan precursors are synthesized in the bacterial cytosol by various enzymes including the ATP-hydrolyzing Mur ligases, which catalyze the stepwise addition of amino acids to a UDP-MurNAc precursor to yield UDP-MurNAc-pentapeptide. MurD catalyzes the addition of D-glutamic acid to UDP-MurNAc-L-Ala in the presence of ATP; structural and biochemical studies have suggested the binding of the substrates with an ordered kinetic mechanism in which ligand binding inevitably closes the active site. In this work, we challenge this assumption by reporting the crystal structures of intermediate forms of MurD either in the absence of ligands or in the presence of small molecules. A detailed analysis provides insight into the events that lead to the closure of MurD and reveals that minor structural modifications contribute to major overall conformation alterations. These novel insights will be instrumental in the development of new potential antibiotics designed to target the peptidoglycan biosynthetic pathway. Crystallographic Study of Peptidoglycan Biosynthesis Enzyme MurD: Domain Movement Revisited.,Sink R, Kotnik M, Zega A, Barreteau H, Gobec S, Blanot D, Dessen A, Contreras-Martel C PLoS One. 2016 Mar 31;11(3):e0152075. doi: 10.1371/journal.pone.0152075., eCollection 2016. PMID:27031227[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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