Enoylpyruvate transferase

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Revision as of 09:37, 11 March 2019

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

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Updated on 11-March-2019

↑ 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

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 == Structural highlights ==
-MurA is composed of <scene name='55/551189/Cv/3'>catalytic domain</scene> and <scene name='55/551189/Cv/5'>C-terminal domain</scene>. The active site is located at the interface of the two domains and binds the <scene name='55/551189/Cv/8'>fosfomycin</scene> and <scene name='55/551189/Cv/7'>UDP-GlcNAc</scene>.<ref>PMID:8994972</ref>
+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/11'>fosfomycin</scene> and <scene name='55/551189/Cv/12'>UDP-GlcNAc</scene>.<ref>PMID:8994972</ref> Water molecules are shown as red spheres.
 </StructureSection>