Mur ligase

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<StructureSection load='2jfg' size='350' side='right' caption='Structure of MurD ligase complex with UMA (stick model), ADP (stick model) and sulfate (PDB entry [[2jfg]])' scene=''>
<StructureSection load='2jfg' size='350' side='right' caption='Structure of MurD ligase complex with UMA (stick model), ADP (stick model) and sulfate (PDB entry [[2jfg]])' scene=''>
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== Function ==
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'''Mur ligase''' are a set of four Mur ubiquitin ligase enzymes: MurC, MurD, MurE, MurF which catalyze the addition of a short polypeptide to UDP-D-acetylmuramic acid in the process of bacterial cell wall buildup from peptidoglycans<ref>PMID:11696548</ref>. All four enzymes are topologically similar and contain N-terminal domain which binds the substrate, an ATP-binding central domain and a C-terminal domain which binds the incorporated amino acid.
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'''MurD ligase''' or '''UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase''' catalyzes the conversion of UDP-N-acetylmuramoyl-L-alanine (UMA), D-glutamate and ATP to UDP-N-acetylmuramoyl-L-alanine-D-glutamate and ADP. MurD is one of four Mur ubiquitin ligase enzymes (MurC, MurD, MurE, MurF) which participate in the biosynthesis of peptidoglycans. All four enzymes are topologically similar and contain N-terminal domain which binds the substrate, an ATP-binding central domain and a C-terminal domain which binds the incorporated amino acid.
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*'''MurC ligase''' or '''UDP-N-acetylmuramoyl-L-alanine ligase''' adds L-alanine to peptidoglycans<ref>PMID:17139082</ref>.
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*'''MurD ligase''' or '''UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase''' catalyzes the conversion of UDP-N-acetylmuramoyl-L-alanine (UMA), D-glutamate and ATP to UDP-N-acetylmuramoyl-L-alanine-D-glutamate and ADP. I.e. adds D-glutamate to peptidoglycans<ref>PMID:18704940</ref>. <br />
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*'''MurE ligase''' or '''UDP-N-acetylmuramoyl-L-alaninyl-D-glutamate-2,6-diaminopimelate ligase''' adds ''meso''-diaminpimelate to peptidoglycans<ref>PMID:212153518</ref>.
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*'''MurF ligase''' or '''UDP-N-acetylmuramoyl-L-alanine-D-glutamyl-lysine-D-alanyl-D-alanine ligase''' adds D-alanyl-D-alanine to peptidoglycans<ref>PMID:23786712</ref>.
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== Relevance ==
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Mur ligases are antibacterial drug targets<ref>PMID:25130693</ref>.
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</StructureSection>
</StructureSection>
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**[[2x5o]], [[2y68]], [[2y66]], [[2y67]], [[2y1o]] – EcMurD + thiazolidine inhibitor <br />
**[[2x5o]], [[2y68]], [[2y66]], [[2y67]], [[2y1o]] – EcMurD + thiazolidine inhibitor <br />
}}
}}
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 08:31, 2 May 2016

Structure of MurD ligase complex with UMA (stick model), ADP (stick model) and sulfate (PDB entry 2jfg)

Drag the structure with the mouse to rotate

3D Structures of MurD ligase

Updated on 02-May-2016

References

  1. ↑ Friedrich R, Fuentes-Prior P, Ong E, Coombs G, Hunter M, Oehler R, Pierson D, Gonzalez R, Huber R, Bode W, Madison EL. Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase. J Biol Chem. 2002 Jan 18;277(3):2160-8. Epub 2001 Nov 5. PMID:11696548 doi:10.1074/jbc.M109830200
  2. ↑ Deva T, Baker EN, Squire CJ, Smith CA. Structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC). Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1466-74. Epub 2006, Nov 23. PMID:17139082 doi:10.1107/S0907444906038376
  3. ↑ Perdih A, Hodoscek M, Solmajer T. MurD ligase from E. coli: Tetrahedral intermediate formation study by hybrid quantum mechanical/molecular mechanical replica path method. Proteins. 2009 Feb 15;74(3):744-59. doi: 10.1002/prot.22188. PMID:18704940 doi:http://dx.doi.org/10.1002/prot.22188
  4. ↑ . PMID:212153518
  5. ↑ Hrast M, Turk S, Sosic I, Knez D, Randall CP, Barreteau H, Contreras-Martel C, Dessen A, O'Neill AJ, Mengin-Lecreulx D, Blanot D, Gobec S. Structure-activity relationships of new cyanothiophene inhibitors of the essential peptidoglycan biosynthesis enzyme MurF. Eur J Med Chem. 2013 May 21;66C:32-45. doi: 10.1016/j.ejmech.2013.05.013. PMID:23786712 doi:10.1016/j.ejmech.2013.05.013
  6. ↑ Kouidmi I, Levesque RC, Paradis-Bleau C. The biology of Mur ligases as an antibacterial target. Mol Microbiol. 2014 Oct;94(2):242-53. doi: 10.1111/mmi.12758. Epub 2014 Sep 5. PMID:25130693 doi:http://dx.doi.org/10.1111/mmi.12758

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