Enoylpyruvate transferase
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | <StructureSection load='3kr6' size='350' side='right' caption='Structure of enoylpyruvate transferase complex with | + | <StructureSection load='3kr6' size='350' side='right' caption='Structure of enoylpyruvate transferase complex with fosfomycin and UDP-N-acetylglucosamine (PDB entry [[3kr6]])' scene=''> |
== Function == | == Function == | ||
| Line 10: | Line 10: | ||
== Structural highlights == | == Structural highlights == | ||
| - | MurA is composed of catalytic domain and C-terminal domain. The active site is located at the interface of the two domains.<ref>PMID:8994972</ref> | + | MurA is composed of catalytic domain and C-terminal domain. The active site is located at the interface of the two domains and binds the fosfomycin and UDP-GlcNAc.<ref>PMID:8994972</ref> |
</StructureSection> | </StructureSection> | ||
Revision as of 17:42, 19 January 2016
| |||||||||||
3D Structures of enoylpyruvate transferase
Updated on 19-January-2016
References
- ↑ Brown ED, Vivas EI, Walsh CT, Kolter R. MurA (MurZ), the enzyme that catalyzes the first committed step in peptidoglycan biosynthesis, is essential in Escherichia coli. J Bacteriol. 1995 Jul;177(14):4194-7. PMID:7608103
- ↑ Skarzynski T, Mistry A, Wonacott A, Hutchinson SE, Kelly VA, Duncan K. Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin. Structure. 1996 Dec 15;4(12):1465-74. PMID:8994972
