2OI5

E. coli GlmU- Complex with UDP-GlcNAc and Acetyl-CoA

Summary for 2OI5

• Entry DOI: 10.2210/pdb2oi5/pdb
• Related: 1HV9 2OI6 2OI7
• Descriptor: Bifunctional protein glmU, MAGNESIUM ION, SULFATE ION, ... (6 entities in total)
• Functional Keywords: left-handed beta helix, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0ACC7
• Total number of polymer chains: 2
• Total formula weight: 101745.38

Authors

Olsen, L.R.,Vetting, M.W.,Roderick, S.L. (deposition date: 2007-01-10, release date: 2007-06-19, Last modification date: 2023-08-30)

Primary citation

Olsen, L.R.,Vetting, M.W.,Roderick, S.L.
Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products.
Protein Sci., 16:1230-1235, 2007

PubMed Abstract: The biosynthesis of UDP-GlcNAc in bacteria is carried out by GlmU, an essential bifunctional uridyltransferase that catalyzes the CoA-dependent acetylation of GlcN-1-PO(4) to form GlcNAc-1-PO(4) and its subsequent condensation with UTP to form pyrophosphate and UDP-GlcNAc. As a metabolite, UDP-GlcNAc is situated at a branch point leading to the biosynthesis of lipopolysaccharide and peptidoglycan. Consequently, GlmU is regarded as an important target for potential antibacterial agents. The crystal structure of the Escherichia coli GlmU acetyltransferase active site has been determined in complexes with acetyl-CoA, CoA/GlcN-1-PO(4), and desulpho-CoA/GlcNAc-1-PO(4). These structures reveal the enzyme groups responsible for binding the substrates. A superposition of these complex structures suggests that the 2-amino group of GlcN-1-PO(4) is positioned in proximity to the acetyl-CoA to facilitate direct attack on its thioester by a ternary complex mechanism.

PubMed: 17473010
DOI: 10.1110/ps.072779707

Experimental method

X-RAY DIFFRACTION (2.25 Å)