Enoylpyruvate transferase
From Proteopedia
(Difference between revisions)
(17 intermediate revisions not shown.) | |||
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='55/551189/Cv/1'> |
== Function == | == Function == | ||
- | '''Enoylpyruvate transferase''' (MurA) catalyzes the ligation of phosphoenolpyruvate (PEP) to UDP-N-acetylglucosamine (UNAG). | + | '''Enoylpyruvate transferase''' ('''MurA''') or '''UDP-N-acetylglucosamine 1-carboxyvinyltransferase''' catalyzes the ligation of phosphoenolpyruvate (PEP) to UDP-N-acetylglucosamine (UNAG). The pyruvate moiety makes the linker between the glycan and peptide portion of peptidoglycans. Thus MurA is essential for the biosynthesis of bacterial cell walls.<ref>PMID:7608103</ref>. |
+ | *'''MurC''' or '''UDP-N-acetylmuramate-L-alanine ligase''' adds L-alanine in the biosynthesis of peptidoglycans which form part of the protective bacterial cell wall<ref>PMID:25114134</ref>. | ||
== Relevance == | == Relevance == | ||
MurA is a target for antibiotics such as fosfomycin. | MurA is a target for antibiotics such as fosfomycin. | ||
- | </StructureSection> | ||
- | == | + | == Structural highlights == |
- | + | MurA is composed of <scene name='55/551189/Cv/9'>catalytic domain</scene> and <scene name='55/551189/Cv/10'>C-terminal domain</scene>. The active site is located at the interface of the two domains and binds the <scene name='55/551189/Cv/15'>fosfomycin</scene> and <scene name='55/551189/Cv/20'>UDP-GlcNAc</scene>.<ref>PMID:8994972</ref> Water molecules are shown as red spheres. | |
- | + | ||
- | + | == 3D Structures of enoylpyruvate transferase == | |
+ | [[Enoylpyruvate transferase 3D structures]] | ||
- | + | </StructureSection> | |
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | **[[3su9]], [[3swa]], [[3swi]] – EncMurA (mutant) + UNAG + PEP<BR /> | ||
- | **[[3swd]] – EcMurA (mutant) + UNAG + PEP<BR /> | ||
- | **[[3swe]] – HiMurA (mutant) + UNAG + PEP<BR /> | ||
- | **[[3swg]] – AaMurA + UNAG + PEP<BR /> | ||
- | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Current revision
|
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
- ↑ Humnabadkar V, Prabhakar KR, Narayan A, Sharma S, Guptha S, Manjrekar P, Chinnapattu M, Ramachandran V, Hameed SP, Ravishankar S, Chatterji M. UDP-N-acetylmuramic acid l-alanine ligase (MurC) inhibition in a tolC mutant Escherichia coli strain leads to cell death. Antimicrob Agents Chemother. 2014 Oct;58(10):6165-71. doi: 10.1128/AAC.02890-14. , Epub 2014 Aug 11. PMID:25114134 doi:http://dx.doi.org/10.1128/AAC.02890-14
- ↑ 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