1UAE

STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE

Summary for 1UAE

• Entry DOI: 10.2210/pdb1uae/pdb
• Descriptor: UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE, URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE, [(1R)-1-hydroxypropyl]phosphonic acid, ... (4 entities in total)
• Functional Keywords: peptidoglycan, transferase, udp-n-acetylglucosamine, fosfomycin
• Biological source: Escherichia coli
• Cellular location: Cytoplasm (Probable): P0A749
• Total number of polymer chains: 1
• Total formula weight: 45618.97

Authors

Skarzynski, T. (deposition date: 1996-09-30, release date: 1997-09-04, Last modification date: 2024-02-14)

Primary citation

Skarzynski, T.,Mistry, A.,Wonacott, A.,Hutchinson, S.E.,Kelly, V.A.,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, 4:1465-1474, 1996

PubMed Abstract: UDP-N-acetylglucosamine enolpyruvyl transferase (MurA), catalyses the first committed step of bacterial cell wall biosynthesis and is a target for the antibiotic fosfomycin. The only other known enolpyruvyl transferase is 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase, an enzyme involved in the shikimic acid pathway and the target for the herbicide glyphosate. Inhibitors of enolpyruvyl transferases are of biotechnological interest as MurA and EPSP synthase are found exclusively in plants and microbes.

PubMed: 8994972
DOI: 10.1016/S0969-2126(96)00153-0

Experimental method

X-RAY DIFFRACTION (1.8 Å)