Mur ligase

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.

3D Structures of MurD ligase

Updated on 02-September-2014

MurD

1e0d – EcMurD – Escherichia coli
3lk7 – MurD – Streptococcus agalactiae
4bub – TmMurD – Thermotoga maritima

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
4bub – TmMurD + ADP

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