Mur ligase: Difference between revisions
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
===MurD=== | |||
[[1e0d]] – EcMurD – ''Escherichia coli'' <br /> | [[1e0d]] – EcMurD – ''Escherichia coli'' <br /> | ||
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[[4bub]] – TmMurD – ''Thermotoga maritima''<br /> | [[4bub]] – TmMurD – ''Thermotoga maritima''<br /> | ||
===MurD complex with ligand=== | |||
[[1uag]], [[1eeh]] – EcMurD + UMA <br /> | [[1uag]], [[1eeh]] – EcMurD + UMA <br /> | ||
Revision as of 07:46, 2 September 2014
<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 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
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman
