Mur ligase
From Proteopedia
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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=''> | ||
| - | '''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 | + | '''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 == | == 3D Structures of MurD ligase == | ||
Revision as of 10:57, 29 July 2014
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