Mur ligase: Difference between revisions
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<StructureSection load='2jfg' size='350' side='right' caption='Structure of MurD ligase complex with UMA, ADP 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=''> | ||
'''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 part of the bacterial peptidoglycan synthesis pathway. | '''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 part of the bacterial peptidoglycan synthesis pathway. | ||
Revision as of 11:07, 22 December 2013
<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=>
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 part of the bacterial peptidoglycan synthesis pathway.
3D Structures of MurD ligase
Updated on 22-December-2013
1e0d – EcMurD – Escherichia coli
3lk7 – MurD – Streptococcus agalactiae
MurD complex with ligand
1uag, 1eeh – EcMurD + UMA
2jfg – EcMurD + UMA + ADP
2uag – EcMurD + UMA + ADP + Mg
3uag – EcMurD + UMA + ADP + Mn
4uag – EcMurD + UAG
MurD complex with inhibitor
2jff, 2jfh, 2uuo, 2uup, 2vtd, 2vte, 2xpc – EcMurD + sulfonamide inhibitor
2wjp – EcMurD + rhodanine inhibitor
2x5o, 2y68, 2y66, 2y67, 2y1o – EcMurD + thiazolidine inhibitor
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman
