1NAW

ENOLPYRUVYL TRANSFERASE

Summary for 1NAW

• Entry DOI: 10.2210/pdb1naw/pdb
• Descriptor: UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYL-TRANSFERASE, CYCLOHEXYLAMMONIUM ION (3 entities in total)
• Functional Keywords: peptidoglycan biosynthesis, hinge, domain movement, sequence motif, folding, transferase
• Biological source: Enterobacter cloacae
• Cellular location: Cytoplasm (Probable): P33038
• Total number of polymer chains: 2
• Total formula weight: 89857.21

Authors

Schoenbrunn, E.,Sack, S.,Eschenburg, S.,Perrakis, A.,Krekel, F.,Amrhein, N.,Mandelkow, E. (deposition date: 1996-07-23, release date: 1997-07-23, Last modification date: 2024-02-14)

Primary citation

Schonbrunn, E.,Sack, S.,Eschenburg, S.,Perrakis, A.,Krekel, F.,Amrhein, N.,Mandelkow, E.
Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin.
Structure, 4:1065-1075, 1996

PubMed Abstract: The ever increasing number of antibiotic resistant bacteria has fuelled interest in the development of new antibiotics and other antibacterial agents. The major structural element of the bacterial cell wall is the heteropolymer peptidoglycan and the enzymes of peptidoglycan biosynthesis are potential targets for antibacterial agents. One such enzyme is UDP-N-acetylglucosamine enolpyruvyltransferase (EPT) which catalyzes the first committed step in peptidoglycan biosynthesis: the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 3-hydroxyl of UDP-N-acetylglucosamine (UDPGlcNAc). EPT is of potential pharmaceutical interest because it is inhibited by the broad spectrum antibiotic fosfomycin.

PubMed: 8805592
DOI: 10.1016/S0969-2126(96)00113-X

Experimental method

X-RAY DIFFRACTION (2 Å)