Enoylpyruvate transferase
From Proteopedia
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== Structural highlights == | == 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/ | + | 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/12'>UDP-GlcNAc</scene>.<ref>PMID:8994972</ref> Water molecules are shown as red spheres. |
== 3D Structures of enoylpyruvate transferase == | == 3D Structures of enoylpyruvate transferase == | ||
Revision as of 11:33, 19 July 2021
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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
