Enoylpyruvate transferase

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<StructureSection load='3swe' size='350' side='right' caption='Structure of enoylpyruvate transferase complex with PEP, UDP-N-acetylglucosamine, glycerol and sulfate (PDB entry [[3swe]])' scene=''>
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<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'>
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== Function ==
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'''Enoylpyruvate transferase''' (MurA) 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 and is a target for antibiotics. MurA is composed of catalytic domain and C-terminal domain.
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'''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>.
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*'''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>.
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== 3D Structures of enoylpyruvate transferase ==
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== Relevance ==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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MurA is a target for antibiotics such as fosfomycin.
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[[1naw]], [[1ejc]], [[1ejd]] – EncMurA – ''Enterobacter cloacae''<BR />
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== Structural highlights ==
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[[1dlg]], [[3spb]], [[3v5v]], [[4e7g]], [[4eii]] – EncMurA (mutant) <BR />
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[[1uae]] – EcMurA – ''Escherichia coli''<BR />
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[[2yvw]] – AaMurA – ''Aquifex aeolicus''<BR />
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[[3zh3]], [[3zh4]] – MurA – ''Streptococcus pneumoniae''<BR />
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===MurA binary complex===
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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.
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[[1a2n]] – EcMurA (mutant) + reaction intermediate<BR />
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== 3D Structures of enoylpyruvate transferase ==
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[[3iss]] – EcMurA (mutant) + enoylpyruvyl-UNAG <BR />
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[[Enoylpyruvate transferase 3D structures]]
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[[1eyn]] – EncMurA (mutant) + aniline-naphthalene sulfonate<BR />
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[[4e7b]] – EncMurA + UDP-glucose<BR />
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[[4e7e]] – EncMurA (mutant) + UDP-glucose<BR />
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[[4e7c]] – EncMurA + UTP<BR />
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[[4e7d]] – EncMurA + UDP<BR />
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[[4e7f]] – EncMurA (mutant) + UDP<BR />
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[[1q3g]] – EncMurA (mutant) + reaction intermediate<BR />
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[[2rl1]] – HiMurA + UNAG – Haemophilus influenzae<BR />
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[[3kqj]] – EcMurA + UNAG <BR />
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[[3upk]] – EncMurA + UNAG <BR />
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[[1ybg]] – EcMurA (mutant) + inhibitor<BR />
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[[3kqa]] – EncMurA + terreic acid inhibitor<BR />
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[[3swq]] – EncMurA (mutant) + enoylpyruvyl-UNAG <BR />
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[[3v4t]] – EncMurA (mutant) + UNAG <BR />
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===MurA ternary complex with antibiotics===
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</StructureSection>
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[[3kr6]] – EcMurA + UNAG + fosfomycin<BR />
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== References ==
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[[3lth]] – EncMurA + UNAG + fosfomycin<BR />
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<references/>
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[[3vcy]] – MurA + UNAG + fosfomycin – ''Vibrio fischeri''<BR />
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[[2rl2]] – HiMurA + UNAG + fosfomycin<BR />
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[[2z2c]] – EcMurA + UNAG + cnicin<BR />
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===MurA ternary complex with PEP===
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[[Category:Topic Page]]
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[[3su9]], [[3swa]], [[3swi]] – EncMurA (mutant) + UNAG + PEP<BR />
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[[3swd]] – EcMurA (mutant) + UNAG + PEP<BR />
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[[3swe]] – HiMurA (mutant) + UNAG + PEP<BR />
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[[3swg]] – AaMurA + UNAG + PEP<BR />
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Current revision

Structure of enoylpyruvate transferase complex with fosfomycin and UDP-N-acetylglucosamine (PDB entry 3kr6)

Drag the structure with the mouse to rotate

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

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Michal Harel, Alexander Berchansky

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