2OI5

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

2OI5 の概要

• エントリーDOI: 10.2210/pdb2oi5/pdb
• 関連するPDBエントリー: 1HV9 2OI6 2OI7
• 分子名称: Bifunctional protein glmU, MAGNESIUM ION, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: left-handed beta helix, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0ACC7
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 101745.38

構造登録者

Olsen, L.R.,Vetting, M.W.,Roderick, S.L. (登録日: 2007-01-10, 公開日: 2007-06-19, 最終更新日: 2023-08-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.25 Å)